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Transient conformational remodeling of folding proteins by GroES - Individually and in concert with GroEL
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering. Institut Fresnel, CNRS UMR 7249, Aix-Marseille Université, Marseille, France.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
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2014 (English)In: Journal of chemical biology, ISSN 1864-6158, E-ISSN 1864-6166, Vol. 7, no 1, 1-15 p.Article, review/survey (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Springer Berlin/Heidelberg, 2014. Vol. 7, no 1, 1-15 p.
Keyword [en]
Carbonic anhydrase; Chaperone; FRET; Molten globule; MreB; Protein folding
National Category
Chemical Sciences Biological Sciences
Identifiers
URN: urn:nbn:se:liu:diva-110534DOI: 10.1007/s12154-013-0106-5PubMedID: 24386013Scopus ID: 2-s2.0-84891782616OAI: oai:DiVA.org:liu-110534DiVA: diva2:746666
Available from: 2014-09-14 Created: 2014-09-12 Last updated: 2017-12-05

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Babu Moparthi, SatishSjölander, DanielVillebeck, LailaJonsson, Bengt-HaraldHammarström, PerCarlsson, Uno

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Babu Moparthi, SatishSjölander, DanielVillebeck, LailaJonsson, Bengt-HaraldHammarström, PerCarlsson, Uno
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