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

Biochemical and Biophysical Research Communications
F Motojima, M Yoshida

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.

References

May 9, 2003·The Journal of Biological Chemistry·Fumihiro Motojima, Masasuke Yoshida
Jan 25, 2005·The Journal of Biological Chemistry·Bei-Wen YingTakuya Ueda
May 15, 2007·Molecular Cell·Nadav EladHelen R Saibil
Oct 21, 2010·The EMBO Journal·Fumihiro Motojima, Masasuke Yoshida
Sep 11, 2012·Proceedings of the National Academy of Sciences of the United States of America·Fumihiro MotojimaMasasuke Yoshida

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Citations

Jul 28, 2018·Journal of Biochemistry·Fumihiro MotojimaMasasuke Yoshida

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