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
Celljournal_title
Cellauthors
Tang YC,Chang HC,Roeben A,Wischnewski D,Wischnewski N,Kerner MJ,Hartl FU,Hayer-Hartl Mdoi
10.1016/j.cell.2006.04.027subject
Has Abstractpub_date
2006-06-02 00:00:00pages
903-14issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(06)00560-5journal_volume
125pub_type
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