ArticleMolecular cell2013
Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.
Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed.
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- Hsp90, DnaK, and ClpB collaborate in protein reactivation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for the dynamic chaperoning of disordered clients by Hsp90.Nature structural & molecular biology · 2024Article
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The role of Aha1 in cancer and neurodegeneration.Frontiers in molecular neuroscience · 2024Review
- Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.Essays in biochemistry · 2023Article
- J-domain Proteins form Binary Complexes with Hsp90 and Ternary Complexes with Hsp90 and Hsp70.Journal of molecular biology · 2023Article
- How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view.Structure (London, England : 1993) · 2023Article
- HtpG Is a Metal-Dependent Chaperone Which Assists the DnaK/DnaJ/GrpE Chaperone System of Mycobacterium tuberculosis via Direct Association with DnaJ2.Microbiology spectrum · 2023Article
- The prophage-encoded transcriptional regulator AppY has pleiotropic effects on E. coli physiology.PLoS genetics · 2023Article
- The development of cancers research based on mitochondrial heat shock protein 90.Frontiers in oncology · 2023Review
- Uncoupling the Hsp90 and DnaK chaperone activities revealed the in vivo relevance of their collaboration in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Global transcriptomic response of Escherichia coli to p-coumaric acid.Microbial cell factories · 2022Article
- Advances towards Understanding the Mechanism of Action of the Hsp90 Complex.Biomolecules · 2022Review
- Hidden information on protein function in censuses of proteome foldedness.Nature communications · 2022Article
- Article
- Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network.Science advances · 2021Article
- The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.Molecular cell · 2021Article
- Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.Genetics · 2021Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors.
Funding
Abstract
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 E. coli Hsp90. The mutant proteins are defective in chaperone activity and client binding in vitro. We constructed homologous mutations in S. cerevisiae Hsp82 and identified several that caused defects in chaperone activity in vivo and in vitro. However, the Hsp82 mutant proteins were less severely defective in client binding to a model substrate than the corresponding E. coli mutant proteins. Our results identify a region in Hsp90 important for client binding in E. coli Hsp90 and suggest an evolutionary divergence in the mechanism of client interaction by bacterial and yeast Hsp90.
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