Abstracts of papers presentedat the 2004 meeting on

MOLECULAR CHAPERONES& THE HEAT SHOCK RESPONSE

May 5-May 9, 2004

Arranged by

James Bardwell, University of MichiganElizabeth Craig, University of Wisconsin, MadisonJonathan Weissman, University of California, San Francisco

Cold Spring Harbor LaboratoryCold Spring Harbor, New York

PROGRAM

WEDNESDAY, May 5—7:30 PM

SESSION 1 DISEASES OF PROTEIN MISFOLDING

Chairperson: S. Lindquist, Whitehead Institute, Cambridge,Massachusetts

Lindauist, S.. Whitehead Institute, Cambridge, Massachusetts: Hsp104and prion inheritance. _ 1

Morimoto, R.I.. Morley, J., Brignull, H., Kim, S., Holmberg, C , Garcia,S., Nollen, E., Plasterk, R., Dept. of Biochemistry, Molecular Biologyand Cell Biology, Rice Institute for Biomedical Research,Northwestern University, Evanston, Illinois; Hubrecht Institute,Utrecht, The Netherlands: Protein misfolding and protein qualitycontrol—Modulators of neurodegenerative diseases and aging. 2

Toogun, T.A., Barnes, J., Bannai, Y., Freeman. B.C., Dept. of Cell andStructural Biology, University of Illinois, Urbana: Dynamic behaviorof genomic complexes induced by the p23 molecular chaperones. 3

Hu, Y., Mivechi, N.F., Institute of Molecular Medicine and Genetics,Dept. of Radiology, Medical College of Georgia, Augusta: Hsf4b—Aheat shock transcription regulated MAP kinase scaffold for a dualspecificity tyrosine phosphotase. 4

Wacker, J.L.,1Zareie, M.H.,2 Sarikaya, M.,2 Muchowski. P.J.,1 Depts.of1 Pharmacology, 2Materials Science and Engineering, Universityof Washington, Seattle: Kinetic destabilization of pre-fibrillar,polyglutamine intermediates by Hsp70 and Hsp40. 5

Chemoff. Y.O., Allen, K.D., Wegrzyn, R.D., Mueller, S., Newnam, G.P.,School of Biology and Institute for Bioengineering and Bioscience,Georgia Institute of Technology, Atlanta: Modulation of prionformation, propagation and aggregation by Hsp levels in yeast.

6Jones, G.,Song, Y., Chung, S., Masison, D.C., Laboratory of

Biochemistry and Genetics, NIDDK. National Institutes of Health,Bethesda, Maryland: Propagation of yeast [PSI+] prion impaired byfactors that regulate Hsp70 substrate binding. 7

Tanaka, M.,1 Chien, P.,1'2 Naber, N.,3 Cooke, R.,3 Weissman, J.S.,1'21 Howard Hughes Medical Institute, Dept. of Cellular and MolecularPharmacology, 2Graduate Group in Biophysics, Dept. ofBiochemistry and Biophysics, University of California, SanFrancisco: Conformational variations in an infectious proteindetermine prion strain differences.

THURSDAY, May 6—9:00 AM

Gross, E.,1 Kaiser, C.,2 Fass, D.,1 1Dept. of Structural Biology,Weizmann Institute of Science, Rehovot, Israel; 2Dept. of Biology,Massachusetts Institute of Technology, Cambridge: Structure ofEroip, source of disulfide bonds for oxidative protein folding in thecell.

Inaba, K.,1'2Takahashi. Y.-h.,1 Ito, K.,1'3 institute for Virus Research,Kyoto University, 2PRESTO, 3CREST, Japan Science andTechnology Corporation: DsbB elicits a red-shift of boundubiquinone during the catalysis of DsbB oxidation.

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SESSION 2 QUALITY CONTROL AND PROTEIN TRAFFICKING

Chairperson: R. Kopito, Stanford University, California

Kopito, R., Stanford University, California.

Nagata, K., Hosokawa, N., Dept. of Molecular Cellular Biology, Institutefor Frontier Medical Sciences, Kyoto University and CREST, JST,Japan: Is EDEM a lectin-like chaperone involved in ERAD?—EDEM, soluble EDEM and more...

Dalbev. R.E., Ohio State University, Columbus: YidC—An essentialprotein involved in membrane protein folding and insertion.

Hendershot, L.M., Meunier, L, Shen, Y., Chung, K.T., Dept. ofGenetics and Tumor Cell Biology, St. Jude Children's ResearchHospital, Memphis, Tennessee: Organization of ER chaperonesand implications for protein folding.

Collet, J.-F.,1 Masip, L.,2 Pan, J.,1 Haldar, S.,3 Penner-Hahn, J.E.,3

Peisach, D.,4 Xu, Z.,4 DeLisa, M.,2 Georgiou, G.,2 Bardwell, J.C.A.,1

Depts. of1 Molecular, Cellular and Developmental Biology,3Chemistry, 4Life Sciences Institute, University of Michigan, AnnArbor; 2Dept. of Chemical Engineering, University of Texas, Austin:An engineered pathway for the formation of protein disulfide bonds.

Furukawa. Y.,1 O'Halloran, T.V.,12 Depts. of 1Chemistry,2Biochemistry, Molecular Biology and Cell Biology, NorthwesternUniversity, Evanston, Illinois: Mild oxidative stress triggers disulfide-based oligomerization of immature forms of superoxide dismutase(SOD1).

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SESSION 3

THURSDAY, May 6—2:00 PM

POSTER SESSION I

Abu-Baker, A., Messaed, C, Laganiere, J., Gaspar, C, Brais, B.,Rouleau, G.A., Center for Research in Neuroscience and HealthCenter, McGill University, Montreal, Canada: Involvement ofmolecular chaperones in oculopharyngeal muscular dystrophy.

Ahrman, E., Nilsson, K., Kucharz, K., Sundby Emanuelsson, C , Dept.of Biochemistry, Lund University, Sweden: Temperature-dependentreversible formation of a small complex between Hsp21 dimers anda model substrate, citrate synthase.

Ahrman, E.,1 Aquilina, A.,2 Robinson, C.,2 Emanuelsson, C.S.,1 1Dept.of Biochemistry, Lund University, Sweden; 2Dept. of Chemistry,University of Cambridge, United Kingdom: Nanoelectrospray massspectrometry shows that the chloroplast small heat shock proteinHsp21 is a dodecamer.

Alanen, H.I..Williamson, R.A.,2 Howard, M.J.,2 Salo, K.E.H.S.,1

Kellokumpu, S.,1 Ruddock, L.W.,1 'Dept. of Biochemistry, Universityof Oulu, Finland; 2Dept. of Biosciences, University of Kent, UnitedKingdom: Functional characterization of human ERp27, a new non-catalytic endoplasmic reticulum located PDI-family member.

Anckar, J.,1'3Hietakangas, V.,3 Denessiouk, K.,2Thiele, D.J.,4

Sistonen, L.,1'3 Depts. of 1Biology, 2Biochemistry and Pharmacy,3Turku Centre for Biotechnology, University of Turku, Abo AkademiUniversity, Finland; 4Dept. of Pharmacology and Cancer Biology,Duke University Medical Center, Durham, North Carolina:Differential sumoylation of HSF1 and HSF2 DNA-binding domains.

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Antoine, W., Stewart, J.M., de los Reyes, B., University of Arkansas,Fayetteville: OsSIH and OsSlt2— Rice orthologs of the Sit genefamily, a new heat shock protein family specific to plants.

Arlander, S.J.H.,1 Toft, D.O.,2 Karnitz, L.M.,1'3'4 Depts. of 1MolecularPharmacology and Experimental Therapeutics, Biochemistry andMolecular Biology, Mayo Graduate Schools, Divs. ofdevelopmental Oncology Research, 4Radiation Oncology, MayoClinic and Foundation, Rochester, Minnesota: Hsp90 inhibitiondepletes Chk1 and sensitizes tumor cells to replication stress.

Atomi, Y.,1 Ohto, E.,1 Yamaguchi, T.,1 Fujita, Y.,1 Harada, T.,2 Tanaka,M.,1 1Dept. of Life Science, University of Tokyo, 2Faculty ofScience, Kyoto University, Japan: Role of aB-crystallin for celldynamics tolerance in muscle cell—Unusual cell/mitochondriamotilities with the antisense modification by time-lapse images.

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Baker, J.P., Rosser, M.F.N., Nicchitta, C.V., Dept. of Cell Biology, DukeUniversity Medical Center, Durham, North Carolina: A stress sensorfunction for GRP94—Adenosine nucleotides and the regulation ofGRP94-client protein interactions. 24

Bali, M.,1 Zhang, B.,1 Ran, F.,1 Morano, K.A.,2 Michels, C.A.,1 Depts. of1 Biology and Biochemistry, Queens College and the GraduateSchool of CUNY, Flushing, New York; 2Dept. of Microbiology andMolecular Genetics, University of Texas Medical School, Houston:The Hsp90 molecular chaperone complex regulates maltoseinduction and stability of the Saccharomyces MAL genetranscription activator.

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Bando, Y., ' Katayama, T., ' Taniguchi, M., ' Tohyama, M., J Dept.of Anatomy, Asahikawa Medical College, 2Dept. of Anatomy andNeuroscience, Osaka University Graduate School of Medicine,3Core Research for Evolutional Science and Technology, JapanScience and Technology (CREST/JST), Saitama: GRP94 (94kDaglucose-regulated protein) suppresses ischemic neuronal cell deathagainst ischemia/reperfusion injury.

Barral, J.M.,1 Agashe, V.R.,1 Guha, S.,1 Chang, H.-C.,1 Genevaux, P.,2

Hayer-Hartl, M.,1 Stemp, M.,1 Georgopoulos, C.,2 Haiti, F.U.,11Dept. of Cellular Biochemistry, Max-Planck Institute ofBiochemistry, Martinsried, Germany; Departement de BiochimieMedicale, Centre Medical Universitaire, Geneve, Switzerland:Different folding pathways in eukaryotes vs. prokaryotes for certainmulti-domain proteins.

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Benaroudj, N., Miot, M., Betton, J.-M., Unit of Protein Folding andModeling, Institut Pasteur, Paris, France: Exploring the biochemicalproperties and interaction of ATP-dependent proteases ClpP1 andClpP2 of M. tuberculosis. 28

Ben-Zvi, A.P.,1 De Los Rios, P.,2 Dietler, G.,3 Goloubinoff, P.,1 1DBMV,Lausanne University, 2Lab. ITP-SB, 3IPMC-SB, EPFL, Lausanne,Switzerland: Hsp70 chaperones unfold stable protein aggregates byactive Brownian strokes. 29

Bharti, K.,1 von Koskull-Doring, P.,1 Bharti, S.,2 Kumar, P.,3 Tintschl-Korbitzer, A.,1 Treuter, E., Nover, L.,1 Depts. of 1Molecular CellBiology, Human Genetics, Cardiovascular Physiology, GoetheUniversity Frankfurt, Germany; 4Dept. of Medical NutritionBiosciences, Karolinska Institute, Stockholm, Sweden: Tomato heatstress transcription factor HsfB1 represents a novel type of generaltranscription coactivator with a histone-like motif interacting withHAC1/CBP. 30

Bitto, E., McKay, D.B., Dept. of Structural Biology, Stanford University,California: Target specificity of the bacterial SurA protein, aperiplasmic chaperone which facilitates outer membrane proteinfolding. 31

Bradley, S., Sheridan Ni Rodaig, C, Shervington, A., Chatfield, L.,Dept. of Forensic and Investigative Science, University of CentralLancashire, Preston, United Kingdom: Post mortem expression ofHsp72 and Hsp27 in porcine skeletal muscle. 32

Breiman, A.,1 Queitsch, C.,2 Sessa, G.,1 Bocovza, S.,1 Aviezer-Hagai,K.,1 Farchi-Pisanty, O.,1 1Dept. of Plant Science, Tel AvivUniversity, Israel; 2Bauer Center for Genomics Research, HarvardUniversity, Cambridge, Massachusetts: The plant co chaperonesFKBPs are heat stress induced and their oyer expression affectsexpression profiles and plant phenotype. 33

Bridges, J.P.,1 Wert, S.E.,1 Nogee, L.M.,2 Weaver, T.E.,1 1Div. ofPulmojiary Biology, Children's Hospital Medical Center, Cincinnati,Ohio; Dept. of Pediatrics, Johns Hopkins University School ofMedicine, Baltimore, Maryland: Accumulation of a misfolded lung-specific protein, sP-CAexon4, causes cytotoxicity. 34

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Brode, S., Javid, B., MacAry, P., Cooke, A., Lehner, P., CambridgeInstitute for Medical Research, Dept. of Pathology, University ofCambridge, United Kingdom: The adjuvanticity of Hsp70—Dissection of in vivo and in vitro activity. 35

Brass, P.,1 Hansen, J.,1 Nielsen, M.N.,1 Kruhoffer, M.,2 Georgopoulos,C.,3 Ang, D.,3 Corydon, T.J.,4 0rntoft, T.,2 Bolund, L.,4 Gregersen,N.,1 1Research Unit for Molecular Medicine, 2Molecular DiagnosticLaboratory, Aarhus University Hospital, 4Dept. of Human Genetics,University of Aarhus, Denmark; 3Centre Medical Universitaire,Geneva, Switzerland: Investigation of the effects of the V72Imutation in human Hsp60 that is associated with hereditary spasticparaplegia.

Brundel, B.J.J.M.,1 Henning, R.H.,2 van Gelder, I.C.,3 Kampinga,H.H.,1 Depts. of1 Radiation and Stress Cell Biology, 2ClinicalPharmacology, University of Groningen, 3Dept. of Cardiology,University Hospital Groningen, The Netherlands: Heat shockproteins protect from myocyte remodeling in human andexperimental atrial fibrillation.

Burch-Smith, T., Dinesh-Kumar, S.P., Dept. of Molecular, Cellular andDevelopmental Biology, Yale University, New Haven, Connecticut:The molecular characterization of Hsp90 functions in plant innateimmunity.

Carrigan, P.E., Roberts, P.J., Smith, D.F., Dept. of Biochemistry andMolecular Biology, Mayo Clinic, Scottsdale, Arizona: Functionalcomparison of human Drosophila Hop.

Carrio, M.M., Villaverde, A., Institut de Biotecnologia i de Biomedicina,Departament de Genetica i de Microbiologia, Universitat Autonomade Barcelona, Spain: Molecular chaperones embedded intobacterial inclusion bodies.

Cescau, S., Chaffotte, A., Debarbieux, L., Delepelaire, P., Sapriel, G.,Wolff, N., Wansdersman, C , Institut Pasteur, Paris, France: SecBdependency of a non Sec substrate—Folding characteristics of theHasA hemophore from S. marcescens via its type I exportergoverns its SecB dependency. 41

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Chadli, A.,1 Graham, J.D.,2 Wood, W.M.,2 Gordon, D.F.,2 Horwitz,K.B.,2 Toft, D.,1 1Dept. of Biochemistry and Molecular Biology, MayoClinic, Rochester, Minnesota; 2Dept. of Endocrinology, University ofColorado Health Sciences Center, Denver: Characterization ofCRIP100—A novel tetratricopeptide repeat protein that interactswith progesterone receptors and Hsp90.

Chang, Y.,1 Trouillet, D.,1 Nykanen, P.,2 Rallu, M.,3 Yorrick, G.,3

Reiner, O.,4 Sistonen, L.,2 Morange, M.,1 Mezger, V.,1 1CRNS UMR8541, Laboratoire de Biologie Moleculaire du Stress, 3CNRS UMR8542, Ecole Normale Superieure, Paris, France; Dept. of Biology,Abo Akademi University and Turku Centre for Biotechnolgy,University of Turku, Finland; 4Dept. of Molecular Genetics,Weizmann Institute, Rehovot, Israel: Mice lacking Hsf2, an atypicalheat shock factor, display neuronal migration defects duringcerebral cortex development.

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Chow, A.M., Anderson, R.L., Peter MacCallum Cancer Center,Melbourne, Australia: Mutational analysis of Hsp72 in the regulationof apoptosis. 44

Compton, S.A.,1 Elmore, L.W.,2 Holt, S.E.,3 Depts. of Vharmacologyand Toxicology, 2Pathology, 3Human Genetics, Massey CancerCenter, Virginia Commonwealth University, Richmond: Hsp90 andp23—A functional association with telomerase and telomeres?

Conlin, L.K., Bulman, A.L., Nelson, H.C.M., Dept. of Biochemistry andBiophysics, University of Pennsylvania School of Medicine,Philadelphia: Structural studies of heat shock factor DNA-bindingdomain mutants.

Connell, P.,1 Christians, E.,2 Soorappan, R.,3 Benjamin, I.,1'3 1Dept. ofInternal Medicine, 2Div. of Cardiology, University of TexasSouthwestern Medical Center, Dallas; 3University of Utah, Salt LakeCity: Role of G6PD-mediated reductive stress in aB-cyrstallincardiomyopathy.

Dou, F.,1 He, H.,2 Llauger, L.,2 Vilenchik, M.,2 Greengard, P.,1 Chiosis,G.,2 Visher Center for Research on Alzheimer's Disease andLaboratory of Molecular and Cellular Neuroscience, RockefellerUniversity, 2Dept. of Medicine, Memorial Sloan-Kettering CancerCenter, New York, New York: Novel Hsp90-interfering agents in thetreatment of neurodegenerative diseases.

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Duennwald, M., Lindquist, S., Whitehead Institute for BiomedicalResearch, Cambridge, Massachusetts: Endoplasmic reticulumstress as a major cause for huntingtin toxicity.

Duong, L.,1 Rewinski, M.,2 McKone, H.,1 Hightower, L.,2 Perdrizet, G.,21St. Joseph College, West Hartford, 2University of Connecticut,Storrs: Clinical assay of stress tolerance—Resistance of red bloodcells to osmotic lysis as an in vivo measure of resistance to stress.

Elguindi, E.C., Toh, S.-M., Blond, S.Y., Center for PharmaceuticalBiotechnology, University of Illinois, Chicago: Ectopic expression ofthe human homolog of endoplasmic membrane-resident Mtj1generates an endoplasmic stress response.

Eriksson, K.K., Vago, R., Calanca, V., Galli, G., Molinari, M., Institutefor Research in Biomedicine, Bellinzona, Switzerland: EDEMcouples ER-associated degradation to protein folding efficiency andsecretory capacity.

Fan, C.-Y., Lee, S., Ren, H.-Y., Cyr, D.M., Dept. of Cell andDevelopmental Biology, University of North Carolina, Chapel Hill:Mechanisms for specification of Hsp70 action by type I and type IIHsp40s.

Felts, S.J.,1 Kim, J.,2 Argon, Y.,3 Chiosis, G.,21Dept. of Biochemistryand Molecular Biology, Mayo College of Medicine, Rochester,Minnesota; 2Dept. of Pathology, University of Pennsylvania,Philadelphia; 3Dept. of Medicine, Memorial Sloan-Kettering CancerCenter, New York, New York: Identification of Hsp90-targetingdrugs having different specificities for various family members.

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Ferguson, S.B., Nelson, H.C.M., Dept. of Biochemistry and Biophysics,University of Pennsylvania School of Medicine, Philadelphia: PKArepresses Hsf1 activity in S. cerevisiae. 55

Flynn, J.M., Levchenko, I., Sauer, R.T., Baker, T.A., Massachusetts v

Institute of Technology, Cambridge: Role of the CIpXP adaptorprotein SspB in the regulation of the extracytoplasmic stressresponse.

Fukuma, M., Allen, J., Sargent, K., Lipson, K:, Urano, F., Programs inGene Function and Expression and Molecular Medicine, Universityof Massachusetts Medical School, Worcester: Endoplasmicreticulum stress in pancreatic p-cells and juvenile diabetes. 57

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Gabai, V.L., Budanova, K., Sherman, M.Y., Boston University School ofMedicine, Massachusetts: Depletion of Hsp72 sensitizes cancercells to radiation, proteasome inhibitors and conventional drugs bydownregulation of ERK and NF-kB signaling pathways. 58

Ghosh, J.G.,1'2 Estrada, M.R.,1 Clark, J.I.,12 '3 Depts. of1 BiologicalStructure, Biomolecular Structure and Design, Ophthalmology,University of Washington, Seattle: Identification of the chaperonesites in human aB crystallin using protein pin arrays.

Giese, K.C., Vierling, E., Dept. of Biochemistry and MolecularBiophysics, University of Arizona, Tucson: Genetic dissection ofsmall heat shock protein function and mechanism in vivo and invitro.

Giraud, Y., Adebayo, J., Stevens, N., Carper, S.W., Dept. of Chemistryand UNLV Cancer Research Center, University of Nevada, LasVegas: Hsp27 inhibits apoptosis induced by an adenosine receptorin human breast cancer cell lines.

Gotoh, T., Oyadomari, S., Tajiri, S., Endo, M., Terada, K., Mori, M.,Dept. of Molecular Genetics, Graduate School of Medical Sciences,Kumamoto University, Japan: Nitric oxide- and ER stress-mediatedapoptosis and its prevention by Hsp70-DnaJ chaperone pairs.

Gottwald, E., Institute for Medical Engineering and Biophysics,Forschungszentrum Karlsruhe, Germany: Intracellular HSP72detection in HL60 cells using a flow cytometry system based onmicrofluidic analysis.

Goussetis, D., Mestril, R., Dept. of Cell Biology, Neurobiology andAnatomy, Program of Molecular and Cellular Biochemistry, LoyolaUniversity of Chicago, Maywood, Illinois: Cardioprotection bymitochondrial heat shock proteins against simulated ischemia. 64

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Guo, Y.,1 Yan, L.-J.,2 Yuhanna, I.S.,3 Christians, E.,2

Sathyanarayanan, S.,2 Moore, G.,2 Gottlieb, R.,4 Robbins, J.,5

Wawrousek, E.,6 Sohal, R.S.,7 Shaul, P.W.,3 Bolli, R.,1 Benjamin,I.J., ' Div. of Cardiology, University of Louisville, Kentucky; Depts.of internal Medicine, 3Pediatrics, University of Texas SouthwesternMedical Center, Dallas; 4Dept. of Molecular and ExperimentalMedicine, Scripps Research Institute, La Jolla, California;Children's Hospital Medical Center, University of Cincinnati, Ohio;

6NEI, National Institutes of Health, Bethesda, Maryland; 7Dept. ofMolecular Pharmacology and Toxicology, University of SouthernCalifornia, Los Angeles; 8University of Utah, Salt Lake City: Novelroles for cytosolic chaperones in mitochondrial nOS expression andROS production. 65

Gupta, S., Knowlton, A.A., Dept. of Cardiovascular Medicine, Universityof California, Davis: Membrane localization of HSP60 in failinghearts. 66

Gur, E.,1 Biran, D.,1 Genevaux, P.,2 Georgopoulos, C.,2 Ron, E.Z.,11Dept. of Molecular Microbiology and Biotechnology, George S.Wise Faculty of Life Sciences, Tel Aviv University, Israel;Departement de Biochimie Medicale, Centre Medical Universitaire,

Universite de Geneve, Switzerland: The E. coli DjIA and CbpAproteins can substitute for DnaJ in DnaK-mediated proteindisaggregation.

Hainzl, O., Wegele, H., Richter, K., Buchner, J.,Technische UniversitatMiinchen, Germany: Cns1, a yeast Hsp90 TPR co-chaperone is anovel activator of the yeast Hsp70 (Ssa1) ATPase.

Hall Skalet, A., King, L.B., Monroe, J.G., Dept. of Pathology andLaboratory Medicine, University of Pennsylvania School ofMedicine, Philadelphia: Qualitative differences in the unfoldedprotein response characterize cell fate decisions of B lymphocytes.

Hamilton, M.G., Giakoumis, M., Ram, P., Kogelman, Y., Oks, M., Dept.of Natural Sciences, Fordham College at Lincoln Center, New York,New York: Searching for Hsp70 in three bivalves—Clams, musselsand oysters.

Hansen, J., Brass, P., Gregersen, N., Research Unit for MolecularMedicine, Aarhus University Hospital and Faculty of HealthSciences, Denmark: Differential handling of wild type medium chainacyl-coA dehydrogenase (MCAD) and a disease-causing mutantvariant by E. coli protein quality control proteases.

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Harada, Y.,1 Sato, C.,1'2 Kitajima, K.,1'2'3 Graduate School ofBioagricultural Science, institute of Advanced Research,3Bioscience Biotechnology Center, Nagoya University, Japan: Aheat shock protein-like, sialic acid-binding lectin on the egg surfaceis involved in the sperm-egg interaction during sea urchinfertilization.

Harris, S.F., Shiau, A.K., Agard, D.A., Howard Hughes MedicalInstitute, Dept. of Biochemistry and Biophysics, University ofCalifornia, San Francisco: Crystal structure of htpG, the E. coliHsp90.

Heikkila, J.J.,1 Kaldis, A.,1 Atkinson, B.G.,2 1Dept. of Biology, Universityof Waterloo, 2Dept. of Biology, University of Western Ontario,Canada: Molecular chaperone function of the R. catesbeianaHSP30.

Hiniker, A.,1 Bardwell, J.C.A.,2 1Medical Scientist Training Program,2Dept. of Molecular, Cellular and Developmental Biology, Universityof Michigan, Ann Arbor: In vivo substrate specificity of periplasmicdisulfide oxidoreductases.

Hoefling, N.,1 Kamal, A.,2 Mestril, R.,1 1Dept. of Cellular and MolecularPhysiology, Loyola University Chicago, Maywood, Illinois;2Conforma Therapeutics Corporation, San Diego, California: Hsp90inhibitors induce the heat shock response and confercardioproteciton against simulated ischemia.

Hollien, J., Weissman, J., University of California, San Francisco:Transcriptional effects of the unfolded protein response inDrosophila cells.

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Harrison, K.L., Juliano, C.E., Hutson, L.D., Dept. of Biology, WilliamsCollege, Williamstown, Massachusetts: Transcriptional regulation ofHSP27, HSPB2 and HSPB3 in developing zebrafish. 74

Haslbeck, M., Braun, N., Stromer, T., Richter, B., Model, N., Weinkauf,S., Buchner, J.,Technische Universitat Miinchen, Germany: Hsp42is the general small heat shock protein in the cytosol of S.cerevisiae. 75

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Hsieh, J.-C, Lee, L., Zhang, L., Wefer, S., Brown, K., DeRossi, C ,Wines, M., Rosenquist, T., Holdener, B.C., State University of NewYork, Stony Brook: The role of MESD in folding the LRP receptorsand specification of mouse embryo polarity.

THURSDAY, May 6—4:30 PM

Wine and Cheese Party

THURSDAY, May 6—7:30 PM

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SESSION 4 CELLULAR RESPONSE TO STRESS

Chairperson: C. Gross, University of California, San Francisco

Gross, C. University of California, San Francisco.

Hartl. F.U.,1 Aqashe, V.R.,1 Guha, S.,1 Chang, H.-C.,1 Geneveaux, P.,2

Hayer-Hartl, M.,1 Stemp, M.>1 Georgopoulos, C.,2 Barral, J.,1 1Dept.of Cellular Biochemistry, Max-Planck Institute of Biochemistry,Martinsried, Germany; 2Departement de Biochimie MedicaleUniversitaire, Universite de Geneve, Switzerland: Protein folding inthe cytosol.

Hultqren. S., Washington University School of Medicine, St. Louis,Missouri.

Winter, J.. Linke, K., Jatzek, A., Hoffmann, J., Jakob, U., Dept. ofMolecular, Cellular and Developmental Biology, University ofMichigan, Ann Arbor: Fighting oxidative heat stress in vivo involvesactivation of Hsp33 and inactivation of DnaK.

Kandror, P., Bretschneider, N., Kreydin, E., Cavalieri, D., Goldberg,A.L., Dept. of Cell Biology, Harvard Medical School, Boston,2Bauer Center for Genomic Research, Harvard University,Cambridge, Massachusetts: Trehalose and certain heat shockproteins are induced at near-freezing temperatures (0 -10 C) andprotect yeast against freezing.

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Mullen J.P.,1 Linde, D.,1 Kcjllner, T.,1 Kawaguchi, S.,2 Vassylyev,D.G., Yokoyama, S.,2 Volkmer-Engert, R.,3 Swaving, J.,4 van Wely,K.,4 Driessen, A.J.M.,4 institute of Molecular Biology, University ofJena, institute for Medical Immunology, Charite, Berlin, Germany;2RIKEN Harima Institute Kouto, Japan; 4Dept. of Microbiology,Groningen Biomolecular Sciences and Biotechnology Institute,University of Groningen, The Netherlands: CsaA proteins—Aneubacterial protein family with chaperone-specific activities. 84

Gong. W.J., Golic, K.G., Dept. of Biology, University of Utah, Salt LakeCity: Loss of Hsp70 in Drosophila is pleiotropic, with effects onthermotolerance, neurodegeneration and aging. 85

Glatz, A.,1 Horvath, I.,1 Balogi, Z.,1 Balogh, G.,1 Puskas, L.G.,1 Josvay,K.,1 Liberek, K.,2 Debreczeny, M.,1 Hunyadi-Gulyas, E.,1

Medzihradszky, K.F.,1 Goloubinoff, P.,3 Viqh, L.,11BiologicalResearch Centre, Szeged, Hungary; 2University of Gdansk, Poland;3University of Lausanne, Switzerland: The emerging role for smallHsps in the regulation of composition and dynamics of cellmembranes. 86

FRIDAY, May 7—9:00 AM

SESSION 5 CHAPERONE FUNCTION IN DISEASE, AGING ANDDEVELOPMENT

Chairperson: R. Morimoto, Northwestern University, Evanston, Illinois

Selkoe, D.J.. Harvard Medical School and Brigham and Women'sHospital, Boston, Massachusetts: Soluble oligomers of misfoldedproteins as diffusible neurotoxins in Alzheimer's and Parkinson'sdiseases. '

Hsu, A., Murphy, C, Kenvon, C, University of California, SanFrancisco: Regulation of aging and age-related disease by DAV016and heat-shock factor.

McClellan, A.J.. Frvdman, J., Dept. of Biological Sciences and BioXProgram, Stanford University, California: Active chaperoneparticipation required for triage of misfolded cytosolic proteins.

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University, Normal: Retinoids assist the cellular folding of theAutosomal Dominant Retinitis Pigmentosa opsin mutant P23H.

Lu. K.P., Finn, G., Lim, J., Pasterino, L., Suizu, F., Sun, A., Wulf, G.,Beth Israel Deaconess Medical Center, Harvard Medical School,Boston, Massachusetts: The prolyl isomerase Pin1—A pivotal newmolecular chaperone in cancer and Alzheimer's disease.

Kim, J.,1 Ou, Y.,2 Esmail, M.,1 Badano, J.,3 Katsanis, N.,3 Rattner, J.,2

Leroux, M.,1 1Dept. of Molecular Biology and Biochemistry, SimonFraser University, Burnaby, 2Dept. of Cell Biology and Anatomy,University of Calgary, Canada 3McKusick-Nathan Institute ofGenetic Medicine, Johns Hopkins University, Baltimore, Maryland:BBS6, a divergent relative of the chaperonin CCT.

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Cheung-Flynn, J., Cox, M.B., Smith, D.F., S.C. Johnson ResearchCenter, Mayo Clinic Scottsdale, Arizona: Targeted disruption of themouse gene for FKBP52, an Hsp90-binding immunophilin, causesabnormal male sexual development consistent with androgeninsensitivity.

Kamal, A.. Sensintaffar, J., Karjian, P., Busch, D., Burrows, F.J.,Conforma Therapeutics Corporation, San Diego, California:Therapeutic implications of Hsp90 activation in cancer and non-oncologic diseases.

Argon, Y..1 Simen, B.B.,2 Ahmed, N.T.,1 Ostrovsky, O.,1 Gidalevitz, T.,2

Wanderling, S.,2 1Dept. of Pathology, Children's Hospital andUniversity of Pennsylvania, Philadelphia; 2Dept. of Pathology,University of Chicago, Illinois: The endoplasmic reticulumchaperone GRP94 is essential for specific differentiation stepsduring development. "2

Noorwez, S.M.,1 Malhotra, R.,1 McDowell, J.H.,1 Smith, K.A.,2 Krebs,M.P.,3 Kaushal. S..1 1Dept. of Ophthalmology, College of Medicine,University of Florida, Gainesville; 2Dept. of Medicine, University ofMinnesota, Minneapolis; 3Dept. of Biological Sciences, Illinois State

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FRIDAY, May 7—2:00 PM

SESSION 6 POSTER SESSION

lizuka, R.,1 So, S.,1 Inobe, T.,2 Yoshida, T.,1 Zako, T.,1 Kuwajima, K.,2

Yohda, M.,1 1Dept. of Biotechnology and Life Sciences, TokyoUniversity of Agriculture and Technology, 2Dept. of Physics,Graduate School of Science, University of Tokyo, Japan: Role ofthe helical protrusion in the conformational change and molecularchaperone activity of the Archaeal group II chaperonin.

Immormino, R., Dollins, D.E., Gewirth, D.T., Dept. of Biochemistry,Duke University Medical Center, Durham, North Carolina: Thestructural basis for ligand regulation in GRP94, the endoplasmicreticulum Hsp90 chaperone.

Inobe, T., Kuwajima, K., Dept. of Physics, University of Tokyo, Japan:<J> value analysis of an allosteric transition of GroEL based on asingle-pathway model.

Inoue, Y.,1Taguchi, H.,2 Yoshida, M.,1 1Chemical ResourcesLaboratory, Tokyo Institute of Technology, 2Dept. of IntegratedBiosciences, Graduate School of Frontier Sciences, University ofTokyo, Japan: Interaction of Hsp104 with yeast prion fibrils.

Iwawaki, T.,1'2 Kohno, K.,1'3 Miura, M.,41Nara Institute of Science andTechnology (NAIST), 2PRESTO, Kawaguchi, 3PROBRAIN, Tokyo,4Graduate School of Pharmaceutical Science, University of Tokyo,Japan: An ER stress-monitoring mouse (ERAI mouse) highlightsthe importance of physiological unfolded protein response in vivo.

Jensen, K.,1 Elmore, L.,2 Holt, S.,1'2'3 Depts. of 1Human Genetics,2Pathology, 3Massey Cancer Center, Virginia CommonwealthUniversity, Richmond: The effect of overexpression of heat shockfactor (HSF1) on telomerase activity and tumorigenicity.

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Johnson, J.L., Weekes, J., Flom, G., University of Idaho, Moscow:Allele-specific interactions of YDJ1 and STI1 and the effect of thesemutations on Hsp90 signaling in S. cerevisiae. 102

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Kapri, E., Adam, Z., Robert H. Smith Institute of Plant Scienes andGenetics in Agriculture, Hebrew University of Jerusalem, Rehovot,Israel: DegP1 protease in Arabidopsis plants—Possible role indegradation of oxidatively damaged membrane proteins.

Kawata, Y., Hongo, K., Uemura, C, Hirai, H., Tsunemi, J., Higurashi,T., Mizobata, T., Dept. of Biotechnology, Faculty of Engineering,Dept. of Biomedical Science, Graduate School of Medical Science,Tottori University, Japan: ATPase/ADPase-dependent chaperoninacitivites of hyperthermophilic group II thermosomes in thepresence of cobalt or manganese ion.

Kenniston, J.A., Baker, T.A., Sauer, R.T., Dept. of Biology,Massachusetts Institute of Technology, Cambridge: The role ofenergy consuption and local protein stability during the substrateprocessing reactions of the CIpXP proteolytic machine.

Kern, R., Malki, A., Liebart, J.-C, Dubucs, C, Yu, M.H., Richarme, G.,Institut Jacques Monod, Universite Paris 7, France: Proteinisoaspartate methyltransferase is a multicopy suppressor of proteinaggregation in E. coli.

Kim, I.,1 Park, T.-G.,1 Kim, Y.H.',1 Cho, J.W.,1 Kang, B.-S.,2 Kim, C-Y.,1 1Dept. of Pharmacology, 2Biomedical Research Institute,Kyungpook National University School of Medicine, Daegu, Korea:Heat-shock response is associated with enhanced contractility ofvascular smooth muscle in isolated rat aorta.

Kim, S.-Y., Craig, E., Dept. of Biochemistry, University of Wisconsin,Madison: Absence of the ribosome-associated Hsp70 chaperoneSsb results in increased cation influx and accumulation.

Kimata, Y., Shimizu, Y., Oikawa, D., Kimata, Y., Kohno, K., NaraInstitute of Science and Technology, Japan: A role of BiP/Kar2 asan adjuster for the ER stress-sensing protein Ire1.

Klein, G., Raina, S., Central Medical University, University of Geneva,Switzerland: Signal transduction pathways in response to proteinmisfolding in the extracytoplasm in E. coli.

Klein, G., Raina, S., Central Medical University, University of Geneva,Switzerland: Altered stress response in a genetic background thatexhibits only conditional synthetic lethality of deletion of both dnaKand tig genes.

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Klein, G., Raina, S., Central Medical University, University of Geneva,Switzerland: Multiple layers of regulation of RpoH including newlydiscovered tyrosine phosphorylation and amino acids within RpoHthat are critical for interaction with dnaK. 112

Kotak, S., Port, M., Ganguli, A., Bicker, F., von Koskull-Doring, P.,Dept. of Molecular Cell Biology, Biocenter, Goethe-UniversityFrankfurt, Germany: The family of Arabidopsis heat stresstranscription factors (Hsf) and the identification of a new signaturecombination of plant class A Hsfs with AHA and NES motifsessential for activator function and intracellular localization. 113

Kovacs, J.J., Yao, T.-P., Dept. of Pharmacology and Cancer Biology,Duke University Medical Center, Durham, North Carolina:Regulation of molecular chaperones by reversible acetylation. 114

Kudla, G.,1 Helwak, A.,2 Lipinski, L.,2 international Institute ofMolecular and Cell Biology, institute of Biochemistry andBiophysics, Warsaw, Poland: Evolution of nucleotide usage inmammalian Hsp70-family genes. 115

Kudla, G.,1 Helwak, A.,2 Gutkowska, M.,3 Walerych, D.,1 Boros, J.,1

Wawrzynow-Zylicz, A.,1 Zylicz, M.,1 international Institute ofMolecular and Cell Biology, institute of Biochemistry andBiophysics, Nencki Institute of Experimental Biology, Warsaw,Poland: Inactivation of a temperature-sensitive p53 mutant byHsp70.

Kwon, H.-Y., Kim, S.-N., Pyo, S.-N., Rhee, D.-K., College of Pharmacy,Sungkyunkwan University, Suwon, Korea: Ca2+ mediatesrepression of CIRCE regulon and hydrophobic surface exposure ofHrcA in S. pneumonias.

Kwon, H.-Y.,1 Ogunniyi, D.,2 Choi, M.-H.,1 Pyo, S.-N.,1 Rhee, D.K.,1

Paton, J.C.,2 1College of Pharmacy, Sungkyunkwan University,Suwon, Korea; 2School of Molecular and Biomedical Science,University of Adelaide, Australia: The CIpP protease ofS. pneumoniae modulates virulence gene expression and protectsagainst fatal pneumococcal challenge.

Lan, C, Lee, H.C., Tang, C, Zhang, L., Dept. of Environmental HealthSciences, Mailman School of Public Health, Columbia University,New York, New York: Two distinct multichaperone complexesmediate the repression and activation of the Heme activator proteinHap1. 119

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Landsverk, M.L.,1 Hutagalung, A.H.,3 Epstein, H.F.,1'2'4 Depts. of1 Biochemistry and Molecular Biology, 2Neurology, Baylor College ofMedicine, Houston, 4Dept. of Neuroscience and Cell Biology,University of Texas Medical Branch, Galveston; 3Dept. of CellBiology, Yale University School of Medicine, New Haven,Connecticut: UCS-domain chaperones target myosin motordomains.

Lappi, A.K.,1 Lensink, M.F.,1 Alanen, H.I.,1 Salo, K.E.H.,1 Lobell, M.,2

Juffer, A.H.,1 Ruddock, L.W.,1 1Dept. of Biochemistry, University ofOulu, Finland; 2Dept. of Biosciences, University of Kent, UnitedKingdom: Proton transfer reactions in the catalytic mechanisms ofPDI.

Lee, A.-H., Iwakoshi, N.N., Glimcher, L.H., Dept. of Immunology andInfectious Diseases, Harvard School of Public Health, Boston,Massachusetts: XBP-1 regulates a subset of endoplasmic reticulumchaperone genes in the unfolded protein response.

Lee, P.,1 Shabbir, A.,1 Cardozo, C.,1 Zhao, Q.,2 Boschelli, F.,2 Arndt,K.,2 Caplan, A.J.,1 1Dept. of Pharmacology and BiologicalChemistry, Mt. Sinai Schoohof Medicine, New York, New York;2Dept. of Oncology, Wyeth-Ayerst Research, Pearl River, NewYork: Role of Hsp90 and Cdc37 in protein kinase folding.

Lee, U., Vierling, E., Dept. of Biochemistry and Molecular Biophysics,University of Arizona, Tucson: Genetic analysis reveals that thecoiled-coil domain of Hsp100/ClpB interacts with NBD1 to play anessential role in thermotolerance.

Lewicki, D., Frausto, S., Zhang, J., Frasier, M., LaFerla, F., Wolozin,B., Loyola University Medical Center, Maywood, Illinois; Universityof California, Irvine: Characterization of transgenic mice over-expressing parkin.

Lubsen, N.H., Doerwald, L., Onnekink, C, van Genesen, ST., deJong, W.W., Dept. of Biochemistry, Faculty of Science, University ofNijmegan, The Netherlands: Translational thermotolerance andsmall heat shock proteins.

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Lundin, V.F.,1 Stirling, P.C.,1 Gomez-Reino, J.,2 Mwenifumbo, J.C.,1

Obst, J.M.,1 Valpuesta, J.M.,2 Leroux, M.R.,1 1Dept. of MolecularBiology and Biochemistry, Simon Fraser University, Burnaby,Canada; 2Centro Nacional de Biotecnologia, CSIC, UniversidadAut6noma de Madrid, Spain: Structure and function of prefoldin—Molecular clamp mechanism of substrate binding.

Luo, S.,1 Baumeister, P.,1 Yang, S.,2 Abcouwer, S.F.,2 Mao, C.,1 Lee,A.S.,1 1Dept. of Biochemistry and Molecular Biology andUSC/Norris Comprehensive Cancer Center, University of SouthernCalifornia Keck School of Medicine, Los Angeles; 2Dept. ofBiochemistry and Molecular Biology, University of New MexicoSchool of Medicine, Albuquerque: The Grp78/Bip promoter isnegatively regulated by a repressive mechanism in vivo.

Ma, Y.,1 Hendershot, L.M.,1'2 1Dept. of Genetics and Tumor CellBiology, St. Jude Children's Research Hospital, 2Dept. of MolecularSciences, University of Tennessee Health Science Center,Memphis: Divergence and convergence of the ER stress responsepathway.

Marcu, M.G.,1 Scroggins, B.T.,1 Wang, D.,2 Cotter, R.J.,2 Neckers, L.,11Urologic Oncology Branch, Center for Cancer Research, NCI,National Institutes of Health, Bethesda, 2Dept. of Pharmacology andMolecular Sciences, Johns Hopkins University School of Medicine,Baltimore, Maryland: Acetylation status of Hsp90 affectscochaperone complexes and client protein association and stability.

Martinez-Hackert, E., Hendrickson, W.A., Howard Hughes MedicalInstitute, Columbia University, New York, New York: Domainfunction, conformational variability and peptide binding ofM. janaschii chaperone W;FKBP26.

Mchaourab, H.S., Koteiche, H.A., Hasige, S.A/, Stein, R.A., Dept. ofMolecular Physiology and Biophysics, Vanderbilt University,Nashville, Tennessee: Mechanistic studies of small heat-shockproteins chaperone activity.

Meinander, A.,12Tran, S.E.F.,13 Sistonen, L.,1'3 Eriksson, J.E.,1'41 9Turku Centre for Biotechnology, Depts. of Biochemistry and

Pharmacy, 3Biology, Abo Akademi University, 4Dept. of Biology,University of Turku, Finland: The death receptor inhibitor FLIP as astress sensor.

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Menezes, R., Amaral, C, Rodrigues-Pousada, C, Genomics andStress Laboratory, Instituto de Tecnologia e Quimica Biologica(ITQB), Oeiras, Portugal: Yap8 regulation in S. cerevisiae underarsenic.

Meriin, A.B., Zhang, X.Q., Sherman, M.Y., Boston University School ofMedicine, Massachusetts: Cellular factors involved in aggregationand toxicity of polypeptides with polyglutamine domains.

Miller, C, Cox, M., Dept. of Environmental Health Sciences, TulaneUniversity Health Sciences Center, New Orleans: Hsp90-p23complexes and Ah receptor signaling.

Miller, V.M.,1|2Gouvion, CM.,1 Rebagliati, M.R.,2'3 Paulson, H.L.,1'21Dept. of Neurology, 2Graduate Program in Genetics, 3Dept. ofAnatomy and Cell Biology, University of Iowa Roy J. and Lucille A.Carver College of Medicine, Iowa City: CHIP suppressespolyglutamine aggregation and toxicity in vitro and in vivo.

Min, J.-N., Zhang, Y., Mivechi, N.F., Institute of Molecular Medicine andGenetics and Dept. of Radiology, Medical College of Georgia,Augusta: Essential role for heat shock transcription factor bindingproteini (Hsbpi) during peri-implantation stage of embryonicdevelopment.

Miyazaki, T., Noguchi, S., Itoh, H., Dept. of Material-ProcessEngineering and Applied Chemistry for Environment, Faculty ofEngineering and Resource Science, Akita University, Japan:Isolation and characterization of mammalian type I and type IIchaperonin.

Mizobata, T.,1'2Taniguchi, M.,1 Yoshimi, T.,2 Hongo, K.,1'2 Kawata,Y.,1'2 1Dept. of Biotechnology, Faculty of Engineering, 2Dept. ofBiomedical Science, Graduate School of Medical Science, TottoriUniversity, Japan: Probing the movements of the GroEL apicaldomain using stopped-flow fluorescence analysis.

Mizrahi, I., Sharkia, R., Bonshtien, A.L., Weiss, C, Niv, A., Lustig, A.,Viitanen, P.V., Azem, A., George S. Wise Faculty of Life Sciences,Tel Aviv University, Israel: Structure-function analysis of thechloroplast chaperonins.

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Montani, N.,1 Tagliavacca, L.,2 Ruffato, E.,2 Pasqualetto, E.,2 Sitia, R.,2

Schiaffonati, L.,1 Fra, A.M.,1 1Dept. of Biomedical Sciences andBiotechnology, University of Brescia, 2Universita Vita-Salute SanRaffaele Scientific Institute, Milano, Italy: How B cells prepare formassive antibody production—Kinetic mRNA analyses of ERresident proteins and Ig subunits.

Motojima, F.,1 Taguchi, H.,2 Yoshida, M.,1 1Chemical ResourcesLaboratory, Tokyo Institute of Technology, 2Dept. of IntegratedBiosciences, Graduate School of Frontier Sciences, University ofTokyo, Japan: Substrate protein refolding in cis cavity of GroEL-GroES-nucleotide complex at high temperature.

Mueller, S.,1 Borschsenius, A.S.,1'2 Patterson, J.,1 Newnam, G.P.,1

Chernoff, Y.O.,1 1School of Biology and Institute of Bioengineeringand Bioscience, Georgia Institute of Technology, Atlanta; 2Dept. ofGenetics and Breeding, St. Petersburg State University, Russia:Effects of homologous and heterologous chaperones on the yeastprion [PSI+].

Neher, S., Flynn, J., Sauer, R.T., Baker, T.A., Dept. of Biology,Massachusetts Institute of Technology, Cambridge: Analysis ofsubstrates of the E. coli CIpXP protease following DNA damage.

Nelson, R.F.,1'2'4 Miller, V.M.,2'3'4 Paulson, H.L.,2'3'4 1Medical ScientistTraining Program, 2Graduate Program in Neuroscience, 3GraduateProgram in Genetics, 4Dept. of Neurology, University of Iowa Roy J.and Lucille A. Carver College of Medicine, Iowa City: Fbx2, a brain-specific F-box protein linked to ER-associated degradation,cooperates with CHIP to reduce mutant polyglutamine protein levelsand aggregates.

Neta-Sharir, I.,1 Lurie, S.,2 Weiss, D.,11Hebrew University, Jerusalem,Israel: The tomato Hsp21 protects photosy3tem II from oxidativedamage and promotes color change during fruit maturation.

Nevitt, T., Pereira, J., Rodrigues-Pousada, C, Genomics and StressLaboratory, Instituto de Tecnologia e Quimica Biologica (ITQB),Oeiras, Portugal: YAP4 gene regulation under osmotic andoxidative stress.

Nielsen, A.K., Rasmussen, M.D., Andersen, J.T., Olsen, P.B., Dept. ofMolecular Biotechnology, Novozymes A/S, Bagsvaerd, Denmark:Transcriptional response of B. licheniformis to heat shock.

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Nieto-Sotelo, J.,Zarate, F., Martinez, L.M., Arroyo, B.L., Instituto deBiotecnologia, Universidad Nacional Autonoma de Mexico,Cuernavaca: Structural-function relationships in the middle region ofS. cerevisiae Hsp104 protein. 150

Niggemann, M., Williams, D.B., University of Toronto, Canada:Polypeptide binding specificity of ER chaperone calnexin. 151

Niikura, Y., Kitagawa, K., Dept. of Molecular Pharmacology, St. JudeChildren's Research Hospital, Memphis, Tennessee: The humanSGT1-HSP90 complex is required for the assembly of kinetochoreprotein complexes. 152

Nikolay, R., Wiederkehr, T., Mayer, M., Bukau, B..ZMBH, University ofHeidelberg, Germany: Biochemical characterization of the humanE3 ligase CHIP and its interaction with Hsc70 and Hsp90. 153

Nishikawa, S.-i.,1 Nakatsukasa, K.,1 Umebayashi, K.,2 Fukuda, R.,3

Endo, T.,1 1Dept. of Chemistry, Graduate School of Science,Nagoya University, 2National Institute of Genetics, Mishima, 3Dept.of Biotechnology, University of Tokyo, Japan: O-mannosylationprevents aggregation of aberrant proteins independently ofendoplasmic reticulum chaperones.

Nishiyama, M., Glockshuber, R., Institute for Molecular Biology andBiophysics, ETH Hbnggerberg, Zurich, Switzerland: Identificationand characterization of the chaperone-subunit complex bindingdomain from the type 1 pilus assembly platform FimD.

Nukina, N.,1 Tanaka, M.,1 Machida, Y.,1 Nishikawa, Y.,2 Akagi, T.,3

Hashikawa, T.,3 Fujisawa, T.,2 laboratory for StructuralNeuropathology, laboratory for Neural Architecture, RIKEN BrainScience Institute, laboratory for Structural Biology, RIKEN HarimaInstitute, Japan: Structural basis for polyglutamine diseasepathogenesis—Therapeutic strategy.

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Ohto, E., Yamaguchi, T., Arai, R., Fujita, Y., Atomi, Y., University ofTokyo, Japan: Striation formation of GFP-aB crystallin in rat beatingcardiac myocyte. 157

XXVI

Pantos, C , Malliopoulou, V., Karamanoli, E., Mourouzis, I.,Sfakianoudis, K., Cokkinos, A.D., Assimacopoulos, P., Varonos, D.,Cokkinos, D.V., 1st Cardiology Dept., Onassis Cardiac SurgeryCenter, Dept. of Pharmacology, University of Athens, Greece: Long-term thyroxine administration results in heat shock protein 27(HSP27) overexpression and protects the heart from ischaemia-reperfusion injury. 158

Pantos, C , Malliopoulou, V., Karamanoli, E., Mourouzis, I.,Sfakianoudis, K., Assimacopoulos, P., Varonos, D., Cokkinos, D.V.,1st Cardiology Dept., Onassis Cardiac Surgery Center, Dept. ofPharmacology, University of Athens, Greece: Involvement of p38MAPK and JNK in the heat stress induced cardioprotection. 159

Peng, C.-W., Kieff, E., Dept. of Medicine and Microbiology andMolecular Genetics, Channing Laboratory, Brigham and Women'sHospital, Harvard Medical School, Boston, Massachusetts:Molecular chaperone and cochaperone coordinately modulate theregulatory function of EBV leader protein LP. 160

Perdrizet, G.,4Enderle, G.,1 Rewinski, M.,4 Kumar, R.,1 Enderle, G.,1

Berman, M.,3 Hightower, L.,2 Depts. of 1Biomedical Engineering,Molecular and Cell Biology, University of Connecticut, Storrs,

3Dept. of Pathology, 4Center for Wound Healing and HyperbaricMedicine, University of Connecticut Health Center and HartfordHospital: HSP70 is proinflammatory in vivo—Implications for chronicwound healing.

Peres Ben-Zvi, A., Kim, S., Morimoto, R., Dept. of Biochemistry,Molecular Biology and Cell Biology, Rice Institute for BiomedicalResearch, Northwestern University, Evanston, Illinois:Polyglutamine aggregate dissociation by human Hsp70. 162

Perng, M.,1 Wen, S.F.,1 van den Ussel, P.,2 Prescott, A.R.,2 Quinlan,R.A.,1 1School of Biological and Biomedical'Sciences, University ofDurham, 2Dept. of Biochemistry, Medical Science Institute,University of Dundee, United Kingdom: Desmin aggregate formationby R120G aB-crystallin is caused by altered filament interaction andis dependent upon network status in cells.

Petrucelli, L., Hutton, M., Mayo Clinic College of Medicine, Rochester,Minnesota: Hsp70 and CHIP regulate tau protein decisions. 164

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Pigaga, V., Quinlan, R.A., School of Biological and BiomedicalSciences, University of Durham, United Kingdom: a-crystallin andprotein misfolding in the eye lens.

Pirneskoski, A.,1'2Klappa, P.,3 Lobell, M.,3 Russell, S.J.,4 Orru, S.,5

Williamson, R.A.,3 Byrne, L.J.,3 Alanen, H.I.,1 Salo, K.E.H.,1

Kivirikko, K.I.,2 Ruoppolo, M.,5 Freedman, R.B.,6 High, S.,4

Ruddock, L.W.,1 Depts. of1 Biochemistry, 2Medical Biochemistryand Molecular Biology, University of Oulu, Finland; 3Dept. ofBiosciences, University of Kent, "School of Biological Sciences,University of Manchester, 6Dept. of Biological Sciences, Universityof Warwick, United Kingdom; CEINGE Biotecnologie Avanzate,Naples, Italy: The primary substrate binding site of the PDI family—Localization, molecular characterization and modulation.

Prince, T., Shao, J., Hartson, S.D., Matts, R.L., Dept. of Biochemistryand Molecular Biology, Oklahoma State University, Stillwater:Hsp90/Cdc37-dependent maturation of protein kinases—Characterization of structure-function relationships that regulatechaperone facilitated kinase biogenesis.

Puorger, C, Vetsch, M., Glockshuber, R., Institute for MolecularBiology and Biophysics, ETH Honggerberg, Zurich, Switzerland:Disassembly of type 1 pilus is kinetically hindered.

FRIDAY, May 7—7:30 PM

SESSION 7 REGULATION OF THE STRESS RESPONSE

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Chairperson: D. Ron, New York University School of Medicine,New York

Marciniak, S., Yun, C, Oyadomari, S., Harding, H.P., Ron, P., Skirball \Institute, New York University School of Medicine, New York:Dualism in the adaptive nature of the unfolded protein response. 169

Mori, K., Kyoto University, Japan.

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Chen, H.-K.,1 Femandez-Funez, P.,2 de Gouyon, B.,3 Lam, Y.C.,1

Kaytor, M.D.,4 Patterson, C.,1 Orr, H.T.,4 Botas, J.,2Zoqhbi, H.Y..1'21Howard Hughes Medical Institute, 2Baylor College of Medicine,Houston, Texas; 3University of North Carolina, Chapel Hill;4University of Minnesota, Minneapolis: Tne role of proteinmodification and degradation in the pathogenesis of SCA1.

Fujimoto, M., Izu, H., Nakamura, K., Takaki, E., Inouye, S., Nakai. A..Depts. of Biochemistry and Molecular Biology, YamaguchiUniversity School of Medicine, Japan: HSF4 regulates proliferationof epithelial cells and differentiation into fiber cells during mouselens development.

Steel, G., Fullerton, D., Tyson, J., Stirling, C, School of BiologicalSciences, University of Manchester, United Kingdom: Coordinationof molecular chaperones in the lumen of the endoplasmic reticulum.

Huang, P.,1|2Gautschi, M.,3 Rospert, S.,3 Craig, E.,1 Depts. ofBiochemistry, 2Biomolecular Chemistry, University of Wisconsin,

Madison; Institut fur Biochemie und Molekularbiologie, UniversitatFreiburg, Germany: Ribosome-associated complex (RAC) as amodulator of Ssb's chaperone function in S.cerevisiae .

Sha. B., Dept. of Cell Biology, Center for Biophysical Sciences andEngineering, University of Alabama, Birmingham: The crystalstructure of the yeast Hsp40 Ydj1 complexed with its peptidesubstrate reveals the mechanism for Hsp40 molecular chaperoneactivity.

SATURDAY, May 8—9:00 AM

SESSION 8 CHAPERONES AND PROTEOLYSIS

Chairperson: T. Baker, Howard Hughes Medical Institute,Massachusetts Institute of Technology, Cambridge

Baker. T.. Howard Hughes Medical Institute, Massachusetts Institute ofTechnology, Cambridge.

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Prakash, S., Tian, L., Mensah, K., Fishbain, S., Jaffe, N.,Koodathingal, P., Matouschek, A., Dept. of Biochemistry, MolecularBiology and Cell Biology and Robert H. Lure ComprehensiveCancer Center, Northwestern University, Evanston, Illinois: Proteinunfolding by the proteasome.

Younger, J.M., Ren, H.-Y., Fan, C.-Y., Patterson, C, Cyr, P.M., Dept.of Cell and Developmental Biology, University of North Carolina,Chapel Hill: Functions for the Hsc70/CHIP E3 ubiquitin ligasecomplex in cell stress protection and protein quality control.

Kostova, Z., Medicherla, B.S., Park, S.-H., Taxis, C, Hitt, R., Wolf,D.H., Institut fur Biochemie, Universitat Stuttgart, Germany: Proteinquality control in the endoplasmic reticulum and the ubiquitin-proteasome-chaperone connection.

Bolon, D.N.,1 Baker, T.A.,1'2 Sauer, R.T.,1 1Dept. of Biology, 2HowardHughes Medical Institute, Massachusetts Institute of Technology,Cambridge: Bivalent tethering of the SspB adaptor to the AAA+protease CIpXP leads to efficient substrate handoff—A proteindesign study.

Isaac. P.P., Silhavy, T.J., Dept. of Molecular Biology, PrincetonUniversity, New Jersey: Regulated periplasmic proteolysis—A rolefor the CpxP protein in combating envelope stress in E. coli.

Forafonov, F.,Picard, P., Dept. of Cell Biology, University of Geneva,Switzerland: The Hsp90 co-chaperone p23 (Sba1) of budding yeast.

Roe, S.M.,1Ali,M.M.U.,1 Meyer, P.,1 Vaughan, C.K.,1 Panaretou, B.,2

Piper, P.W.,3 Prodromou, C.,1 Pearl, L.H.,1 1Section of StructuralBiology, Institute of Cancer Research, Chester Beatty Laboratories,2Div. of Life Sciences, King's College London, 3Dept. ofBiochemistry and Molecular Biology, University College London,United Kingdom: The structure of the C-terminal domain of p50 inthe complex with the N-terminal domain of Hsp90 and the \mechanism of regulation by p50.

Shirasu, K.. Azevedo, C, Takahashi, A., Peart, J., Casais, C ,Ichimura, K., Sainsbury Laboratory, John Innes Centre, Norwich,United Kingdom: Chaperone complex in plant disease resistance.

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SESSION 9

SATURDAY, May 8—2:00 PM

POSTER SESSION

Rabinovich, E., Shapira, I., Elkabetz, Y., Alalouf, G., Bar-Nun, S., Dept.of Biochemistry, Tel Aviv University, Israel: Cytosolic chaperonesessential for ERAD.

Raden, D.,1 Hildebrandt, S.,2Xu, P.,1 Bell, E.,1 Doyle, F.J.,2 Robinson,A.S.,1 1Dept. of Chemical Engineering, University of Delaware,Newark; 2Dept. of Chemical Engineering, University of California,Santa Barbara: Analysis and modeling of BiP/Kar2p in the unfoldedprotein response.

Rakwalska, M., Rospert, S., Institute of Biochemistry and MolecularBiology, University of Freiburg, Germany: Function of ribosome-associated complex (RAC) in translation fidelity.

Rauch, T.,1 Hundley, H.,2 Kramer, G.,1 Vorderwulbecke, S.,1 Pfund,C.,2 Bukau, B.,1 Craig, E.A.,2 Peuerling, E.,1 1Zentrum furMolekulare Biologie (ZMBH), Universitat Heidelberg, Germany;2Dept. of Biochemistry, University of Wisconsin, Madison:Understanding the function and mechanism of ribosome-associatedchaperones of yeast and E. coli.

Riggs, D.L., Smith, P.F., Pept. of Biochemistry and Molecular Biology,Mayo Clinic Scottsdale, Arizona: Steroid hormone signaling isregulated by the Hsp90 co-chaperone FKBP52 in yeast andmammalian cells.

Roos-Mattjus, P.,1'3Nykanen, P.,2'3 Bjork, J.,1'3 Akerfelt, M.,1'3 Plotka,M.,3 Sistonen, L.,1' Pepts. of 1Biology, 2Biochemistry andPharmacy, Abo Akademi University, Turku,Centre for Biology, AboAkademi University and University of Turku, Finland: HSF2 bindingto the hsp70 promoter requires the presence of HSF1.

R6ttgers, K., von Janowsky, B., Krayl, M., Voos, W., Institut furBiochemie und Molekularbiologie, Universitat Freiburg, Germany:Molecular characterization of the degradation properties of themitochondrial AAA+ protease Pim1.

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Rousseau, E.,1 Pehay, B.,1 Ben-HaTem, L.,2 Trottier, Y.,2 Morange,M.,1 Bertolotti, A., 1Laboratoire de Genetique Moleculaire, CNRSUMR8541, Ecole Normale Superieure, Paris, Institut de Genetiqueet de Biologie Moleculaire et Cellulaire, INSERM-CNRS, UniversiteLouis Pasteur, Illkirch, France: Aggregation of expandedpolyglutamine proteins is modulated by subcellular environment.

Rowley, G.,1 Miticka, H.,4 Humphreys, S.,1 Fookes, M.,2 Thompson,A., Stevenson, A.,1 Rezuchova, B.,4 Ivens, A.,2 Hinton, J.,Kormanec, J.,4 Roberts, M.,11University of Glasgow, 2SangerInstitute, Cambridge, United Kingdom; Institute of Food Research,Institute of Molecular Biology, Bratislava, Slovakia: S. typhimurium

rpoE regulon.

Rudella, A.,1 Peltier, J.-B.,1 Ripoll, P.,2 Friso, G.,1 Cai, Y.,1 Ytterberg,J.,1 Giacomelli, L.,1 van Wijk, K.J.,1 Pepts. of Vlant Biology,Theory and Simulation Sciences and Engineering, Cornell

University, Ithaca, New York: CIp protease complexes from plastidsand mitochondria of plants, their predicted 3-D structures andfunctional implications—A reverse genetics and proteomicsapproach.

Riidiger, S., Freund, S.M.V., Fersht, A.R., Cambridge Centre forProtein Engineering, Cambridge University and Medical ResearchCouncil, United Kingdom: Monitoring interactions of Hsp90 with itssubstrate p53 and ATP at the molecular level using NMR andsegmental labeling.

Rujano, M.A., Kampinga, H.H., Salomons, F.A., Dept. of Radiation andStress Cell Biology, Faculty of Medical Sciences, University ofGroningen, The Netherlands: The Hsp70 chaperone machine andthe dynamics of poly-Q inclusion formation.

Russell, L.,1 Morishima, Y.,2 Pratt, W.,2 Chinkers, M.,1 1Dept. ofPharmacology, University of South Alabama, Mobile; University of\Michigan, Ann Arbor: An unexpected role for the Hsp organizerprotein (Hop) in glucocorticoid regulation in living cells.

Satpute, P., Serio, T., Dept. of Molecular Biology, Cell Biology andBiochemistry, Brown University, Providence, Rhode Island: Sup35prion conversion timing in vivo.

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I Schaffar, G.,1 Breuer, P.,1 Boteva, R.,2 Behrends, C.,1 Tzvetkov, N.,1

I Sakahira, H.,1 Siegers, K.,1 Hayer-Hartl, M.,1 Hartl, F.U.,1 1Dept. ofI ; Cellular Biochemistry, Max-Planck-lnstitute of Biochemistry,§i Martinsried, Germany; Institute of Molecular Biology, BulgarianII Academy of Sciences, Sofia: Cellular toxicity of polyglutamine-§1 expansion proteins—Mechanism of transcription factor deactivation. 1 ^ 7

j l Schlothauer, T., Dougan, D.A., Kirstein, J., Mogk, A., Bukau, B.,I Turgay, K., Zentrum fur Molekulare Biologie, Universitat Heidelberg,I Germany: Adaptor protein controlled oligomerization activates the| AAA+ protein CIpC. 198

^Sevier, C.S.,1 Vala, A.,1 Gross, E.,2 Fass, D.,2 Kaiser, C.A.,1 1Dept. ofI.; Biology, Massachusetts Institute of Technology, Cambridge; 2Dept.

of Structural Biology, Weizmann Institute of Science, Rehovot,Israel: Intracellular mechanisms for specific disulfide bond formationand transfer between proteins. 199

Shaner, L.,1 Trott, A.,1 Goeckeler, J.L.,2 Brodsky, J.L.,2 Morano, K.A.,11Dept. of Microbiology and Molecular Genetics, University of TexasMedical School, Houston; 2Dept. of Biological Sciences, Universityof Pittsburgh, Pennsylvania: The function of the yeast molecularchaperone Sse1 is mechanistically distinct from the closely relatedHsp70 family. 2 0 0

Sheridan Ni Rodaig, C, Bradley, S., Shervington, A., Chatfield, L.,Dept. of Forensic and Investigative Science, University of CentralLancashire, Preston, United Kingdom: Post mortem expression ofHsp72 and Hsp27 in porcine skin. 201

Shimohata, N., Akiyama, Y., Ito, K., Institute for Virus Research, KyotoUniversity, Japan: SecY alterations that lead to abnormalmembrane protein assembly. 202

Song, C.,1'2 Wang, Q.,2 Li, C.-C.,1'21SAIC-Frederick, laboratory ofCancer Prevention, CCR, NCI, National Institutes of Health,Bethesda, Maryland: Chaperone activity of p97-VCP in preventingprotein aggregation. 203

Sorensen, S., Ranheim, T., Leren, T.P., Kulseth, M.A., Dept. ofMedical Genetics, Rikshospitalet University Hospital, Oslo, Norway:Accumulation of mutant LDL-receptor in ER leads to ER-stress. 204

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Sorgjerd, K.,1 Jonsson, B.-H.,1 Kelly, J.W.,2 Blond, S.Y.,3

Hammarstrom, P.,1 1IFM-Dept. of Chemistry, Linkoping University,Sweden; 2Skaggs Institute of Chemical Biology and Dept. ofChemistry, Scripps Research Institute, La Jolla, California; 3Centerfor Pharmaceutical Biotechnology, Dept. of Medicinal Chemistryand Pharmacognosy, College of Pharmacy, University of Illinois,Chicago: The chaperone BiP binds the highly amyloidogenic CNSdisease associated transthyretin mutant D18G.

Soti, C , Sreedhar, A.S., Kalmar, E., Petak, I., Csermely, P., Depts. ofMedical Chemistry and Pathology, Semmelweis University,Budapest, Hungary: A novel drug binding-site of Hsp90.

Sriburi, R.,1 Jackowski, S.,2 Mori, K.,3 Brewer, J.W.,1 1Dept. ofMicrobiology and Immunology, Stritch School of Medicine, LoyolaUniversity Chicago, Maywood, Illinois; 2Div. of Protein Science,Dept. of Infectious Diseases, St. Jude Children's Research Hospital,Memphis, Tennessee; 3Dept. of Biophysics, Graduate School ofScience, Kyoto University, Japan: XBP1—A link between theunfolded protein response and lipid biosynthesis.

Sriburi, R.,1 Jackowski, S.,2 Mori, K.,3 Brewer, J.W.,1 1Dept. ofMicrobiology and Immunology, Stritch School of Medicine, LoyolaUniversity, Maywood, Illinois; 2Div. of Protein Science, Dept. ofInfectious Diseases, St. Jude Children's Research Hospital,Memphis, Tennessee; 3Dept. of Biophysics, Graduate School ofScience, Kyoto University, Japan: Evidence that XBP1 functions asa master regulator of the exocytic pathway.

Stockton, J.D., Merkert, M.C., Kellaris, K.V., University of California,Berkeley: Chaperones on the wrong site of the fence—CytosolicBiP and PDI family members and their affect on translocation of theprion protein.

Strbuncelj, M., Kusmierczyk, A., Serio, T., Dept. of Molecular Biology, v

Cellular Biology and Biochemistry, Brown University, Providence,Rhode Island: Quality control of co-translational folding andinteraction with the Sup35 prion cycle. 210

Summer, H., Bruderer, R., Weber-Ban, E., Institute for MolecularBiology and Biophysics, ETH Honggerberg, Zurich, Switzerland:Isolation and characterization of a new AAA-protein from A.fulgidus. 211

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Terada, K.,1 Yomogida, K.,2 Imai, T.,2 Kiyonari, H.,3 Takeda, N.,4

Kadomatsu, T., Yano, M.,1 Aizawa, S.,3 Mori, M.,1 1Dept. ofMolecular Genetics, Graduate School of Medical Science, 4Div. ofTransgenic Technology, CARD, Kumamoto University, 2Dept. ofScience for Laboratory Animal Exp. Research Institute for MicrobialDiseases, Osaka University, laboratory for Animal Research andGenetics Engineering, RIKEN, CDB, Japan: Defect ofspermiogenesis in DjA1 cochaperone knockout mouse.

Thibault, G., Djokic, J., Houry, W.A., Dept. of Biochemistry, Universityof Toronto, Canada: Substrate recognition and degradation byCIpXP chaperone-protease complex of £. coli.

Tiberio, L.,1 Fenaroli, A.,1 Maroni, P.,2 Bendinelli, P.,2 Piccoletti, R.,2

Schiaffonati, L.,1 1Pipartimento di Scienze Biomediche eBiotecnologie, Universita degli Studi di Brescia, 2lstituto di PatologiaGenerale, Universita degli Studi di Milano, Italy: In vivo heat shockresponse in the brain—Signaling pathway and transcription factoractivation.

Tkach, J.M., Smith, L.-L.S., Glover, J.R., Pept. of Biochemistry,University of Toronto, Canada: Effect of subcellular distribution onHsp104 function.

Tomoyasu, T., Sasaki, T., Takaya, A., Yamamoto, T., Pept. ofMicrobiology and Molecular Genetics, Graduate School ofPharmaceutical Sciences, Chiba University, Japan: A novel smallHSP "AgsA" which is involved in suppressing protein aggregation inS. typhimurium.

Trindade, L.M., Horvath, B.M., Bergervoet, M., Visser, R.G.F.,Graduate School of Experimental Plant Sciences, Laboratory ofPlant Breeding, Pept. of Plant Sciences, Wageningen University,The Netherlands: Isolation of a gene encoding a copper chaperonefor the Cu/Zn superoxide dismutase and characterization of itspromoter in S. tuberosum.

Tummala, H.,1 Jung, C.,1 Tiwari, A.,2 Higgins, C.,2 Trang, E.,1

Hayward, L.,2 Xu, Z.,1 Pepts. of 1Biochemistry and MolecularPharmacology, 2Neurology, University of Massachusetts MedicalSchool, Worcester: Inhibition of chaperone activity is a gainedproperty of SOD1 mutants that cause amyotrophic lateral sclerosis.

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Uryu, K.,1 Richter-Landsberg, C.,2 Welch, W.J.,3 Pham, C.T.,1 Sun,E.,1 Giasson, B.,1 Lee, V.M.-Y.,1 Trojanowski, J.Q.,1 1CenterforNeurodegenerative Disease Research, Dept. of Pathology andLaboratory Medicine, University of Pennsylvania School ofMedicine, Philadelphia; Dept. of Biology, Molecular Neurobiology,University of Oldenburg, Germany; Dept. of Medicine andPhysiology, University of California, San Francisco: Association ofHsp90 with a-synuclein lesions in synucleinopaties.

Valgardsdottir, R., Chiodi, I., Giordano, M., Cobianchi, F., Riva, S.,Biamonti, G., Istituto di Genetica Molecolare, Consiglio Nazionaledelle Ricerche, Pavia, Italy: Nuclear stress bodies as largetranscription factories.

Van Molle, W.,1 Sekikawa, K.,2 Jaattela, M.,3 Kollias, G.,4 Libert, C.,11Dept. for Molecular Biomedical Research, Ghent University,Belgium; 2Dept. of Molecular Biology and Immunology, NationalInstitute of Agrobiological Sciences, Tsukuba, Japan; institute ofCancer Biology, Danish Cancer Society, Copenhagen; Institute ofImmunology, Biological Sciences Research Center AlexanderFleming, Vari, Greece: HSP70 has strong in vivo anti-inflammatorycapacities—Lessons froni Hsp70.1 knockout and Hsp70 transgenicmice.

Vang, S.,1 Corydon, T.J.,2 Borglum, A.,2 Scott, M.D.,3 Frydman, J.,3

Gregersen, N.,1 Brass, P.G.,1 1Research Unit for MolecularMedicine, Aarhus University Hospital and Faculty of HealthSciences, institute of Human Genetics, University of Aarhus,Denmark; Dept. of Biological Sciences, Stanford University,California: Actin mutations causing hypertrophic and dilatedcardiomyopathy exhibit decreased protein stability and prolongedinteraction with the TRiC/CCT chaperonin.

Vilaboa, N.,1 Fenna, M.,2 Munson, J.,3 Roberts, S.M.,3 Voellmy, R.,21 Research Unit, Hospital Universitario La Paz, Madrid, Spain;2Pept. of Biochemistry and Molecular Biology, University of MiamiSchool of Medicine, Florida; 3Dept. of Environmental and HumanToxicology, University of Florida, Gainesville: Novel heat andligand-controlled switches for targeting and timing expression oftransferred genes.

Villebeck, L., Hammarstrom, P., Lindgren, M., Jonsson, B.-H., IFM,Linkoping, Sweden: Is the chaperonin TRiC an unfoldase?

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Walerych, P.,1'4 Kudla, G.,1'4 Gutkowska, M.,3 Helwak, A.,2Zylicz, M.,1

Wawrzynow-Zylicz, A.,1 international Institute of Molecular and CellBiology, UNESCO-PAS, institute of Biochemistry and Biophysics,institute of Experimental Biology, Polish Academy of Sciences,4School of Molecular Medicine, Warsaw, Poland: Hsp90chaperones a wild-type p53 tumor suppressor protein. 225

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Wandinger, S., Wegele, H., Buchner, J., Institut fur Organische Chemie& Biochemie, Technische Universitat Munchen, Germany:Regulation of the Hsp90 system by co-chaperones. 226

Welsh, M.J.,1 Hirano, S.,1 Sun, X.,1 Ransom, R.F.,2 Smoyer, W.E.,2

Shelden, E.A.,3 Benndorf, R.,1 Pepts. of 1Cell and PevelopmentalBiology, Pediatrics and Communicative Piseases, University ofMichigan Medical School, Ann Arbor; 3School of MolecularBiosciences, Washington State University, Pullman: p38MAPK/HSP25-signaling regulates cadmium-induced contraction ofmesangial cells.

Westerheide, S., Bosman, J., Kawahara, T., Matsumoto, G., Kim, S.,Silverman, R., Morimoto, R., Pept. of Biochemistry, MolecularBiology and Cell Biology, Rice Institute for Biomedical Research,Northwestern University, Evanston, Illinois: Celastrols as inducersof the human heat shock response and cellular cytoprotection.

Wiegant, F.A.C.,1 Vorontsova, O.N.,2 Manukhina, E.B.,2 Malyshev,l.Y.,2 1Pept. of Molecular Cell Biology, Utrecht University, TheNetherlands; 2Pept. of Adaptive Biology and Medicine, Institute ofGeneral Pathology and Pathophysiology, Moscow, Russia:Tolerance and gradual development of adaptation as two differentforms of temperature response.

Wirth, P.,1 Bureau, F.,2 Melotte, P.,2 Gustin, P.,1 Christians, E.,31Unitof Pharmacology, Pharmacotherapy and Toxicology, 2Unit ofPhysiology, Pept. of Functional Sciences, Faculty of VeterinaryMedicine, University of Liege, Belgium; 3Center of DevelopmentalBiology, University Paul Sabatier, Toulouse, France: Role of heatshock factor 1 in lung protection.

Wochnik, G.,1 Young, J.C.,2 Holsboer, F.,1 Hartl, F.U.,2 Rein, T.,1

Max-Planck Institute of Psychiatry, 2Max-Planck Institute ofBiochemistry, Munich, Germany: Inhibition of GR-mediatedtranscription by p23 requires interaction with Hsp90.

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Xing, H.,1 Mayhew, C.N.,3 Cullen, K.E.,1 Park-Sarge, O.-K.,2 Sarge,K.D.,1 Depts. of 1Molecular and Cellular Biochemistry, 2Physiology,Chandler Medical Center, University of Kentucky, Lexington; 3Dept.of Cell Biology, Neurobiology and Anatomy, University of Cincinnati,Ohio: HSF1 functions as both transcriptional activator andpolyadenylation stimulatory factor, enhancing Hsp expression at twodifferent steps of the gene expression pathway.

Xu, W., Yuan, X., Mimnaugh, E., Neckers, L., Urologic OncologyBranch, Center for Cancer Research, NCI, National Institutes ofHealth, Bethesda, Maryland: Hsp90 binding is correlated withkinase activity and geldanamycin-sensitivity of ErbB2 tyrosinekinase.

Yamamoto, K.,1'2 Yoshida, H.,2'3 Kokame, K.,4 Kaufman, R.J.,5'6 Mori,K.,2 1 Graduate School of Biostudies, 2Dept. of Biophysics, GraduateSchool of Science, Kyoto University, Japan 3PRESTO, JapanScience and Technology Corporation, Saitama, 4NationalCardiovascular Center Research Institute, Osaka, Japan; 5HowardHughes Medical Institute, 6Dept. of Biological Chemistry, Universityof Michigan Medical Center, Ann Arbor: Involvement of ATF6 andXBP1 in activating endoplasmic reticulum stress-responsive cis-acting element ERSE-II.

Yano, M.,Terada, K., Mori, M., Kumamoto University, Japan:Chaperone-like functions of a new cytosolic factor AIP andmitochondrial Tom20 mediate mitochondrial protein import.

Yohda, M.,1 Usui, K.,1 Hatipoglu, O.F.,1 Ishii, N.,21Tokyo University ofAgriculture and Technology, National Institute of AdvancedIndustrial Science and Technology, Tsukuba, Japan: Structural andfunctional characterization of two small heat shock proteins fromS. tokodaii strain 7.

Yoshida, H.,1'2 Mori, K.,2 1PRESTO, Japan Science and Technology \Corporation, 2Graduate School of Science, Kyoto University, Japan:Transcriptional induction of XBP1 pre-mRNA by the ATF6 pathwayis crucial for activation of the IRE1-XBP1 pathway in mammalianER stress response.

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i Yoshida, T.,1 Urushida, Y.,2 lizuka, R.,1 Maruyama, T.,3 Yohda, M.,11Dept. of Biotechnology and Life Sciences, Tokyo University ofAgriculture and Technology, 2Marine Biotechnology Institute Co.Ltd., Iwate, 3Dept. of Marine Ecosystems Research, Japan MarineScience and Technology Center (JAMSTEC), Yokosuka: Closure ofthe built-in lid in archaeal group II chaperonin is triggered by ATPbinding.

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, B.-G., Huang, W., Leach, N., Hartson, S.D., Matts, R.L., Dept. ofBiochemistry and Molecular Biology, Oklahoma State University,Stillwater: Novobiocin induces a distinct conformation of Hsp90 andalters Hsp90-cochaperone-client interactions.

**•' iMco, T.,1'2 Nomura, T.,1 lizuka, R.,1 Ueno, T.,2 Funatsu, T.,2 Yohda,i- M.,11Dept. of Biotechnology and Life Science, Tokyo University of

Agriculture and Technology, 2Dept. of Physics, School of Scienceand Technology, Waseda University, Japan: Kinetic analysis ofinteractions between archaeal prefoldin and substrate proteins.

Zaltsman, A.,1 Raskind, A.,1 Feder, A.,1 Sakamoto, W.,2 Adam, Z.,11Robert H. Smith Institute of Plant Sciences and Genetics inAgriculture, Hebrew University of Jerusalem, Israel; 2ResearchInstitute for Bioresources, Okayama University, Japan: The family ofchloroplast FtsH protease in Arabidopsis—Expression and function.

Zhang, K.,1 Wong, H.N.,1 Song, B.,2 Miller, C.N.,1 Scheuner, D.,2

Kaufman, R.J.,1'2 1Dept. of Biological Chemistry, 2Howard HughesMedical Institute, University of Michigan Medical Center, Ann Arbor:The unfolded protein response—An intracellular signaling essentialfor B lymphopoiesis.

Zhao, R.,1 Davey, M.,2 Hsu, Y.-C.,1 Kaplanek, P.,1 Tong, A.,2 Parsons,A.,2 Krogan, N.,2 Cagney, G.,2 Mai, D.,2 Greenblatt, J.,2 Boone, C.,2

Emili, A.,2 Houry, W.A.,1 1Dept. of Biochemistry, 2Program inProteomics and Bioinformatics, Banting and Best Dept. of MedicalResearch, University of Toronto, Canada: An integrative cellularnetwork of physical, genetic and chemical-genetic interactions ofyeast Hsp90 chaperone.

Zhou, J., Xu, Z., Life Science Institute and Dept. of BiologicalChemistry, University of Michigan Medical School, Ann Arbor:Structural determinants of SecB recognition by SecA in bacterialprotein translocation.

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Zuiderweg, E.R.P., Zhang, Y., Revington, M., Berjanskii, M.V.,Semenchenko, V., Holder, T., Kurochkin, A.V., Depts. of BiologicalChemistry, Chemistry and Biophysics, University of Michigan, AnnArbor: Structural biology of Hsp70s and complexes with co-chaperones in solution.

Zurawski, D.V., Stein, M.A., Dept. of Microbiology and MolecularGenetics, University of Vermont, Burlington: The SPI2-encodedSseA chaperone has discrete domains required for SseBstabilization and export, and binds within the C-terminus of SseBand SseD.

SATURDAY, May 8—6:00 PM

CONCERTGrace Auditorium

Mikhail Simonyan, violinistAlexei Podkorytov, piano

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PROGRAMSuite in Old Style

Sonata for Violin and Piano

Sonata No. 3 in D Minor

Alfred Schnittke(b. 1934)

Francis Poulenc(1895-1963)

Johannes Brahms(1862-1918)

Russian violinist Mikhail Simonyan is recognized as a leading talent of hisgeneration. He was invited to perform with the National Symphony for theKennedy Center's Anniversary Gala in April 2001 by nationally acclaimedconductor, Leonard Slatkin, and then again at Wolf Trap in the summer of 2002.Mikhail has also performed with the Russian National Orchestra, the MoscowChamber Orchestra, the Jupiter Symphony, the Novosibirsk Philharmonic, andthe Moscow Virtuosi led by Vladimir Spivakov. His 2004 engagements willinclude a solo recital debut at the Kennedy Center. He is currently living in NewYork and studying with Victor Danchenko.

Russian native Alexei Podkorytov began studying piano at the age of four and byseven, he had entered the Special School of Music for Children. He gave his firstpublic performance one year later and continued to tour throughout Russia as arecital pianist and as a soloist with numerous orchestras. Mr. Podkorytov haswon First Prize at the Siberian Piano Competition in Novosibirsk and receivedThird Prize in the International Competition in Senigallia, Italy. In 2002, Alexeisoloed with the American Russian Young Artists Orchestra on its fifteenthanniversary World Tour, performing the Scriabin Piano Concerto. He is currentlystudying for his master's degree at The Juilliard School of Music.

SATURDAY, May 8

BANQUET

Cocktails 7:00 PM Dinner 7:45 PM

SUNDAY, May 9—9:00 AM

CHAPERONE BIOCHEMISTRY AND PROTEINFOLDING

irson: B. Bukau, Universitat Heidelberg, Germany

B.,1 Schlieker, C.,1 Weibezahn, J.,1 Tessarz, P.,1 Tsai, F.,2

Mogk, A.,1 1Universitat Heidelberg, Germany; 2Dept. ofBiochemistry and Molecular Biology, Baylor College of Medicine,Houston, Texas: Substrate recognition by the AAA+ chaperoneCIpB.

"Jjfarausee. S., University of California, Berkeley.

Harwich. A.L.1 Farr, G.W.,1 Ranson, N.A.,2 Sabil, H.R.,2 Fenton,$ W.A., Motojima, F.,1 1Howard Hughes Medical Institute, Dept. of

j ; Genetics, Yale University School of Medicine, New Haven,'X. Connecticut; 2Dept. of Crystallography, Birkbeck College, London,

United Kingdom: Folding triggered at GroEL—A "power stroke" ofapical domain movement driven by ATP/GroES binding overcomesa load imposed by substrate polypeptide on the apical domains.

• Shewmaker, F.,1'2Kerner, M.J.,3 Hayer-Hartl, M.,3 Klein, G.,2

Georgopoulos, C.,2 Landrv. S.J.. 1Pept. of Biochemistry, TulaneUniversity Health Sciences Center, New Orleans, Louisiana;Departement de Biochimie Medicale, University of Geneva,

':• Switzerland; 3Pept. of Cellular Biochemistry, Max-Planck Institut furBiochemie, Martinsried, Germany: A mobile loop order-disorder

'{'• transition modulates the speed of chaperonin cycling.

.- tin, Z.,Rye. H.S.. Pept. of Molecular Biology, Princeton University,New Jersey: Expansion and compression of a protein foldingintermediate by GroEL.

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I-Ludlam, A.V.. Moore, B.A., Xu, Z., Pept. of Biochemistry, Life Sciences

Institute, University of Michigan, Ann Arbor: Crystal structure of thebacterial ribosome bound chaperone trigger factor at 2.5 Angstromresolution. 251

Lee, S.,1 Sowa, M.E.,1 Watanabe, Y.-h.,2 Yoshida, M.,2 Tsai, F.T.F..1

Verna and Marrs McLean Pept. of Biochemistry and MolecularBiology, Baylor College of Medicine, Houston, Texas; 2ChemicalResources Laboratory, Tokyo Institute of Technology, Japan: Thestructure of CIpB—A molecular chaperone that rescues proteinsfrom an aggregated state. 252

Buchner, J., Stomer, T., Saibil, H% Haslbeck, M., Pept. of Chemistry,Technische Universitat Mtinchen, Germany: Structure and functionof small heat shock proteins. 253

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