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

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.

authors

Motojima F,Yoshida M

doi

10.1016/j.bbrc.2015.08.108

subject

Has Abstract

pub_date

2015-10-09 00:00:00

pages

72-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(15)30500-3

journal_volume

466

pub_type

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