Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL

The commonly accepted dogma of the bacterial GroE chaperonin system entails protein folding mediated by cycles of several ATP-dependent sequential steps where GroEL interacts with the folding client protein. In contrast, we herein report GroES-mediated dynamic remodeling (expansion and compression)...

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Bibliographic Details
Published in:Journal of chemical biology 2014, Vol.7 (1), p.1-15
Main Authors: Moparthi, Satish Babu, Sjölander, Daniel, Villebeck, Laila, Jonsson, Bengt-Harald, Hammarström, Per, Carlsson, Uno
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Binding sites
Biochemistry
Biological and Medical Physics
Biophysics
Cell Biology
Chemistry
Chemistry and Materials Science
Opinion Paper
Pharmacology/Toxicology
Physical Chemistry
Protein folding
Proteins
Stress response
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Summary:The commonly accepted dogma of the bacterial GroE chaperonin system entails protein folding mediated by cycles of several ATP-dependent sequential steps where GroEL interacts with the folding client protein. In contrast, we herein report GroES-mediated dynamic remodeling (expansion and compression) of two different protein substrates during folding: the endogenous substrate MreB and carbonic anhydrase (HCAII), a well-characterized protein folding model. GroES was also found to influence GroEL binding induced unfolding and compression of the client protein underlining the synergistic activity of both chaperonins, even in the absence of ATP. This previously unidentified activity by GroES should have important implications for understanding the chaperonin mechanism and cellular stress response. Our findings necessitate a revision of the GroEL/ES mechanism.
ISSN:1864-6158
1864-6166
1864-6166
DOI:10.1007/s12154-013-0106-5