Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions.

Mujacic, Mirna; Bader, Martin W; Baneyx, François

Mujacic, Mirna; Bader, Martin W; Baneyx, François.

Affiliation

Mujacic M; Department of Bioengineering, University of Washington, Box 351750, Seattle, WA 98195, USA.

Mol Microbiol ; 51(3): 849-59, 2004 Feb.

Article in En | MEDLINE | ID: mdl-14731284

Subject(s)

Bacterial Proteins/metabolism; Escherichia coli Proteins/metabolism; Heat-Shock Proteins/metabolism; Molecular Chaperones/metabolism; Protein Folding; Cell Division; Cell Survival; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; HSP40 Heat-Shock Proteins; Hot Temperature; Models, Molecular; Molecular Chaperones/genetics

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Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Protein Folding / Molecular Chaperones / Escherichia coli Proteins / Heat-Shock Proteins Language: En Journal: Mol Microbiol Journal subject: BIOLOGIA MOLECULAR / MICROBIOLOGIA Year: 2004 Document type: Article Affiliation country: United States Country of publication: United kingdom

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