Article
Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.
Molecular cell - 7 Feb 2013
Genest Olivier, Reidy Michael, Street Timothy O, Hoskins Joel R, Camberg Jodi L, Agard David A, Masison Daniel C, Wickner Sue
Abstract excerpt
The heat shock protein 90 (Hsp90) family of heat shock proteins is an abundantly expressed and highly conserved family of ATP-dependent molecular chaperones. Hsp90 facilitates remodeling and activation of hundreds of proteins. In this study, we developed a screen to identify Hsp90-defective mutants in E. coli. The mutations obtained define a region incorporating residues from the middle and C-terminal domains of...
Topics
- Amino Acid Sequence
- Amino Acids
- Escherichia coli
- Escherichia coli Proteins
- HSP90 Heat-Shock Proteins
- Molecular Sequence Data
- Mutant Proteins
- Mutation
- Protein Binding
- Protein Structure, Tertiary