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Molecular Chaperones & Stress Responses Abstracts of papers presented at the 2010 meeting on MOLECULAR CHAPERONES & STRESS RESPONSES May 4–May 8, 2010 CORE Metadata, citation and similar papers at core.ac.uk Provided by Cold Spring Harbor Laboratory Institutional Repository Cold Spring Harbor Laboratory Cold Spring Harbor, New York Abstracts of papers presented at the 2010 meeting on MOLECULAR CHAPERONES & STRESS RESPONSES May 4–May 8, 2010 Arranged by F. Ulrich Hartl, Max Planck Institute for Biochemistry, Germany David Ron, New York University School of Medicine Jonathan Weissman, HHMI/University of California, San Francisco Cold Spring Harbor Laboratory Cold Spring Harbor, New York This meeting was funded in part by the National Institute on Aging; the National Heart, Lung and Blood Institute; and the National Institute of General Medical Sciences; branches of the National Institutes of Health; and Enzo Life Sciences, Inc. Contributions from the following companies provide core support for the Cold Spring Harbor meetings program. Corporate Sponsors Agilent Technologies Life Technologies (Invitrogen & AstraZeneca Applied Biosystems) BioVentures, Inc. Merck (Schering-Plough) Research Bristol-Myers Squibb Company Laboratories Genentech, Inc. New England BioLabs, Inc. GlaxoSmithKline OSI Pharmaceuticals, Inc. Hoffmann-La Roche Inc. Sanofi-Aventis Plant Corporate Associates Monsanto Company Pioneer Hi-Bred International, Inc. Foundations Hudson-Alpha Institute for Biotechnology Front cover, top: HSP90, a regulator of cell survival. Inhibition of HSP90 activity by drugs like geldanamycin (GA) destabilizes client proteins which ultimately lead to the onset of apoptosis. Dana Haley-Vicente, Assay Designs (an Enzo Life Sciences company). Front cover, bottom: C. elegans expressing a proteotoxic polyglutamine- expansion protein. Richard Morimoto, Northwestern University. Back cover, clockwise from top left: Maltose binding protein (translucent), shown suspended in its molten globule state with chaperone protein SecB (yellow), destined for transport across the cellular membrane. Philipp Bechtluft, Arnold Driessen, Sander Tans and Graham Johnson. Nuclear localization of Hsp10 in cultured human lung fibroblasts. The image shows Hsp10 in the cytoplasm and in the nucleus of most cells in a culture of the human lung fibroblast cell line, HLF-1. The chaperonin is considered a mitochondrial protein but here we demonstrate by immunohistochemistry that it also occurs in the cytoplasm and in the nucleus. Bar = 50 microns. Simona Corrao. University of Palermo. Structure of the oligomeric small heat shock protein, alphaB-Crystallin, determined by solid-state NMR. The structure reveals that the C-terminus IXI motif from one unit in the oligomer binds in the substrate-binding groove of a neighboring until, suggesting an auto-inhibitory mechanism for chaperone activity. Rachel Klevit, University of Washington. Artwork prepared by S. Jehle. Structure of the protein alpha-crystallin determined by electron microscopy. Johannes Buchner, Technische Universität München. Several ribosomes (brown) are shown translating a messenger RNA (gray). As the elongating nascent protein (orange) emerges from the ribosome, it undergoes limited folding, but interactions with the exit tunnel and the surrounding area (shaded red) prevent the acquisition of stable tertiary structure. The ribosome effectively acts as a chaperone to prevent premature folding and misfolding of the nascent chain. After release from the ribosome, the free protein folds into its native structure (large orange structure). These conclusions are based on our single molecule force spectroscopy data probing the folding state of ribosome- associated nascent chains. Christian Kaiser, University California, Berkeley. MOLECULAR CHAPERONES & STRESS RESPONSES Tuesday, May 4 – Saturday, May 8, 2010 Tuesday 7:30 pm 1 Chaperone Biochemistry and Protein Folding Wednesday 9:00 am 2 Chaperone Function in Disease and Development Wednesday 2:00 pm 3 Poster Session I Wednesday 4:30 pm Wine and Cheese Party * Wednesday 7:30 pm 4 Evolution and Regulation of Protein Folding Machines Thursday 9:00 am 5 Manipulating Chaperone Networks and Protein Folding Pathways Thursday 2:00 pm 6 Poster Session II Thursday 7:30 pm 7 Chaperones and Proteolysis Friday 9:00 am 8 Diseases of Protein Misfolding Friday 2:00 pm 9 Poster Session III Friday 6:00 pm Concert 7:00 pm Banquet Saturday 9:00 am 10 Quality Control and Protein Trafficking Poster sessions are located in Bush Lecture Hall * Airslie Lawn, weather permitting Mealtimes at Blackford Hall are as follows: Breakfast 7:30 am-9:00 am Lunch 11:30 am-1:30 pm Dinner 5:30 pm-7:00 pm Bar is open from 5:00 pm until late Abstracts are the responsibility of the author(s) and publication of an abstract does not imply endorsement by Cold Spring Harbor Laboratory of the studies reported in the abstract. These abstracts should not be cited in bibliographies. Material herein should be treated as personal communications and should be cited as such only with the consent of the author. Please note that recording of oral sessions by audio, video or still photography is strictly prohibited except with the advance permission of the author(s), the organizers, and Cold Spring Harbor Laboratory. Printed on 100% recycled paper. PROGRAM TUESDAY, May 4—7:30 PM SESSION 1 CHAPERONE BIOCHEMISTRY AND PROTEIN FOLDING Chairperson: J. Bardwell, Howard Hughes Medical Institute, University of Michigan, Ann Arbor Protein stabilization by selection James Bardwell. Presenter affiliation: University of Michigan, Ann Arbor, Michigan. 1 Trajectory of ATP-induced domain movements in GroEL Dan Clare, Daven Vasishtan, Maya Topf, Joel Quispe, George Farr, Art Horwich, Helen Saibil. Presenter affiliation: Birkbeck College of London, United Kingdom. 2 Role of molecular chaperones in SOD1-linked ALS Arthur Horwich, Wayne Fenton, Krystyna Furtak, Maria Nagy, Urmi Bandyopadhyay, Navneet Tyagi. Presenter affiliation: Yale School of Medicine, New Haven, Connecticut. 3 Chaperonin-catalyzed rescue of entropically trapped states in protein folding Kausik Chakraborty, Jyoti Sinha, Manal Chatila, Qiaoyun Shi, Bernhard C. Poschner, Martin Sikor, Guoxin Jiang, Don C. Lamb, F-Ulrich Hartl, Manajit Hayer-Hartl. Presenter affiliation: Max Planck Institute of Biochemistry (MPIB), Martinsried, Germany; Institute of Genomics and Integrative Biology (CSIR), Delhi, India. 4 Single molecule analysis of nascent protein folding Christian M. Kaiser, Daniel H. Goldman, Susan Marqusee, Carlos Bustamante. Presenter affiliation: University of California, Berkeley, Berkeley, California. 5 v Taming the beast—Structural biology of a small heat shock protein Rachel E. Klevit, Stefan Jehle, Benjamin Bardiaux, Katja Dove, Barth von Rossum, Hartmut Oschkinat, Ponni Rajagopal. Presenter affiliation: University of Washington, Seattle, Washington. 6 Three-dimensional structure of the Hsp104 AAA+ ATPase Francis T. Tsai, Sukyeong Lee, Bernhard Sielaff, Jungsoon Lee. Presenter affiliation: Baylor College of Medicine, Houston, Texas. 7 Rapid folding completion in the cage or escaping out of the cage—Alternative fates of substrate polypeptide interacting with GroEL/GroES interface region in the critical intermediate of chaperonin-assisted folding Fumihiro Motojima, Masasuke Yoshida. Presenter affiliation: Kyoto Sangyou University, Kyoto, Japan. 8 WEDNESDAY, May 5—9:00 AM SESSION 2 CHAPERONE FUNCTION IN DISEASE AND DEVELOPMENT Chairperson: E. Deuerling, University of Konstanz, Germany Functions and mechanisms of cytosolic chaperones in protein homeostasis Elke Deuerling, Ansgar Koplin, Steffen Preissler, Yulia Ilina, Miriam Koch, Annika Scior. Presenter affiliation: University of Konstanz, Konstanz, Germany. 9 The heat shock response— Integrated neuronal networks for metabolic control, stress, and aging Richard I. Morimoto, Anat Ben-Zvi, Veena Prahlad, Laetitia Chauve. Presenter affiliation: Northwestern University, Evanston, Illinois. 10 Insights into Hsp90-client protein interactions from NMR H. Jane Dyson, Sung Jean Park, Maria A. Martinez-Yamout. Presenter affiliation: The Scripps Research Institute, La Jolla, California. 11 vi The Hsp110 molecular chaperone modulates dynein activity Taras Makhnevych, Philip Wong, Oxana Pogoutse, Franco J. Vizeacoumar, Yolanda Chong, Charles Boone, Andrew Emili, Walid A. Houry. Presenter affiliation: University of Toronto, Toronto, Canada. 12 The role of small Heat Shock Proteins in protein folding diseases Serena Carra, Alessandra Boncoraglio, Melania Minoia, Bart Kanon, Jeanette F. Brunsting, Marianne P. Zijlstra, Michel J. Vos, Ody C. Sibon, Harm H. Kampinga. Presenter affiliation: UMCG & RuG, Groningen, Netherlands. 13 How do intrinsically unfolded chaperones work? Dana Reichmann, Marianne Ilbert, Ying Xu, Claudia M. Cremers, Michael C. Fitzgerald, Ursula Jacob. Presenter affiliation: University of Michigan, Ann Arbor, Michigan. 14 The interplay between chaperones, prion protein dynamics and their cellular context Is crucial for protein-only inheritance Tricia Serio, Aaron Derdowski, Susanne DiSalvo, Courtney Klaips, Suzanne Sindi. Presenter affiliation: Brown University, Providence, Rhode Island. 15 Conserved conformational states and cochaperone interactions define the Hsp90 molecular chaperone cycle Daniel R. Southworth, David A. Agard. Presenter affiliation: University of California, San Francisco, San Francisco, California. 16 WEDNESDAY, May 5—2:00 PM SESSION 3 POSTER SESSION I SRR—A novel type of Hsp90-related supra-domain associated with neurodegeneration
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