The C-terminal Tails of the Bacterial Chaperonin GroEL Stimulate Protein Folding by Directly Altering the Conformation of a Substrate Protein

• Published in: The Journal of biological chemistry Vol. 289; no. 33; pp. 23219 - 23232
• Main Authors: Weaver, Jeremy, Rye, Hays S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.08.2014; American Society for Biochemistry and Molecular Biology
• Subjects: Chaperonin 10 - chemistry; Chaperonin 10 - genetics; Chaperonin 10 - metabolism; Chaperonin 60 - chemistry; Chaperonin 60 - genetics; Chaperonin 60 - metabolism; Escherichia coli - chemistry; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Oligopeptides; Protein Binding; Protein Folding; Protein Structure and Folding; Protein Structure, Tertiary; Chaperonin; Protein Misfolding; Hsp60; GroEL; Chaperone; Molecular Chaperone; Protein Dynamic; Protein Folding

Many essential cellular proteins fold only with the assistance of chaperonin machines like the GroEL-GroES system of Escherichia coli. However, the mechanistic details of assisted protein folding by GroEL-GroES remain the subject of ongoing debate. We previously demonstrated that GroEL-GroES enhance...