Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

Abstract:

:GroEL and GroES form a chaperonin nano-cage for proteins up to approximately 60 kDa to fold in isolation. Here we explored the structural features of the chaperonin cage critical for rapid folding of encapsulated substrates. Modulating the volume of the GroEL central cavity affected folding speed in accordance with confinement theory. Small proteins (approximately 30 kDa) folded more rapidly as the size of the cage was gradually reduced to a point where restriction in space slowed folding dramatically. For larger proteins (approximately 40-50 kDa), either expanding or reducing cage volume decelerated folding. Additionally, interactions with the C-terminal, mildly hydrophobic Gly-Gly-Met repeat sequences of GroEL protruding into the cavity, and repulsion effects from the negatively charged cavity wall were required for rapid folding of some proteins. We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways.

journal_name

Cell

journal_title

Cell

authors

Tang YC,Chang HC,Roeben A,Wischnewski D,Wischnewski N,Kerner MJ,Hartl FU,Hayer-Hartl M

doi

10.1016/j.cell.2006.04.027

subject

Has Abstract

pub_date

2006-06-02 00:00:00

pages

903-14

issue

5

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(06)00560-5

journal_volume

125

pub_type

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