Transient conformational remodeling of folding proteins by GroES - Individually and in concert with GroEL

Linköpings universitet, Kemi Linköpings universitet, Tekniska fakulteten Linköpings universitet, Tekniska högskolan Linköpings universitet, Molekylär Bioteknik Institut Fresnel, CNRS UMR 7249, Aix-Marseille Université, Marseille, France 2014

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.

Carbonic anhydrase; Chaperone; FRET; Molten globule; MreB; Protein folding; Chemical Sciences; Kemi; Biological Sciences; Biologiska vetenskaper; Article, review/survey; info:eu-repo/semantics/article; text

10.1007.s12154-013-0106-5

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UPE oai:DiVA.org:liu-110534
0000-0001-5827-3587
doi:10.1007/s12154-013-0106-5
PMID 24386013
Scopus 2-s2.0-84891782616
1234550468

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