GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?

Victor V Marchenkov; Gennady V Semisotnov

doi:10.3390/ijms10052066

GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?

Int J Mol Sci. 2009 May 12;10(5):2066-2083. doi: 10.3390/ijms10052066.

Authors

Victor V Marchenkov¹, Gennady V Semisotnov¹

Affiliation

¹ Institute of Protein Research, Russian Academy of Sciences, 142290, Russian Federation, Pushchino, Moscow Region, Institutskaya street, 4, Russia.

Abstract

The folding of protein molecules in the GroEL inner cavity under the co-chaperonin GroES lid is widely accepted as a crucial event of GroEL-assisted protein folding. This review is focused on the data showing that GroEL-assisted protein folding may proceed out of the complex with the chaperonin. The models of GroEL-assisted protein folding assuming ligand-controlled dissociation of nonnative proteins from the GroEL surface and their folding in the bulk solution are also discussed.

Keywords: GroEL/ES chaperonin system; chaperones; protein aggregation; protein folding.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Adenosine Triphosphate / metabolism
Binding Sites
Chaperonin 10 / metabolism
Chaperonin 10 / ultrastructure
Chaperonin 60 / metabolism*
Chaperonin 60 / ultrastructure*
Escherichia coli / metabolism
Protein Binding
Protein Conformation
Protein Folding*

Substances

Chaperonin 10
Chaperonin 60
Adenosine Triphosphate