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. 2015 Oct 9;466(1):72-5.
doi: 10.1016/j.bbrc.2015.08.108. Epub 2015 Aug 29.

Productive folding of a tethered protein in the chaperonin GroEL-GroES cage

Fumihiro Motojima  1 , Masasuke Yoshida  2
Affiliations

Productive folding of a tethered protein in the chaperonin GroEL-GroES cage

Fumihiro Motojima et al. Biochem Biophys Res Commun. .

Abstract

Many proteins in bacterial cells fold in the chaperonin cage made of the central cavity of GroEL capped by GroES. Recent studies indicate that the polypeptide in the cage spends the most time as a state tethered dynamically to the GroEL/GroES interface region, in which folding occurs in the polypeptide segments away from the tethered site (F. Motojima & M. Yoshida, EMBO J. (2010) 29, 4008-4019). In support of this, we show here that a polypeptide in the cage tethered covalently to an appropriate site in the GroEL/GroES interface region can fold to a near-native structure.

Keywords: Chaperonin; Cysteine-mediated cross-linking; GroEL; Molecular chaperone; Protein folding.

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