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Moparthi SB, Sjölander D, Villebeck L, et al. Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL. J Chem Biol. 2013;7(1):1-15doi: 10.1007/s12154-013-0106-5.
Moparthi, S. B., Sjölander, D., Villebeck, L., Jonsson, B. H., Hammarström, P., & Carlsson, U. (2013). Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL. Journal of chemical biology, 7(1), 1-15. https://doi.org/10.1007/s12154-013-0106-5
Moparthi, Satish Babu, et al. "Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL." Journal of chemical biology vol. 7,1 (2013): 1-15. doi: https://doi.org/10.1007/s12154-013-0106-5
Moparthi SB, Sjölander D, Villebeck L, Jonsson BH, Hammarström P, Carlsson U. Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL. J Chem Biol. 2013 Oct 05;7(1):1-15. doi: 10.1007/s12154-013-0106-5. eCollection 2013. PMID: 24386013; PMCID: PMC3877409.
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J Chem Biol. 2013 Oct 05;7(1):1-15. doi: 10.1007/s12154-013-0106-5. eCollection 2013.

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

Journal of chemical biology

Satish Babu Moparthi, Daniel Sjölander, Laila Villebeck, Bengt-Harald Jonsson, Per Hammarström, Uno Carlsson

Affiliations

  1. IFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden ; Institut Fresnel, CNRS UMR 7249, Aix-Marseille Université, Ecole Centrale Marseille, Marseille, France.
  2. IFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden.

PMID: 24386013 PMCID: PMC3877409 DOI: 10.1007/s12154-013-0106-5

Abstract

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.

Keywords: Carbonic anhydrase; Chaperone; FRET; Molten globule; MreB; Protein folding

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