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Uncovering a Region of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast
Authors:Olivier Genest  Michael Reidy  Timothy O Street  Joel R Hoskins  Jodi L Camberg  David A Agard  Daniel C Masison  Sue Wickner
Institution:1. Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA;2. Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA;3. Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA;4. The Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158, USA
Abstract:
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  • Highlights? Using a genetic screen, we selected for defective mutants of E. coli Hsp90 ? The mutants are impaired in ATP-dependent chaperone activity ? The mutations define a client-binding region of E. coli Hsp90 ? Mutation of homologous residues in yeast Hsp90 causes in vivo and in vitro defects
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