The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin.

Abstract:

:Chaperones, a group of proteins that assist the folding of other proteins, seem to work in a coordinated manner. Two major chaperone families are heat-shock protein families Hsp60 and Hsp70. Here we show for the first time the formation of a stable complex between chaperonin-containing TCP-1 (CCT) and Hsc70, two eukaryotic representatives of these chaperone families. This interaction takes place between the apical domain of the CCT beta subunit and the nucleotide binding domain of Hsc70, and may serve to deliver the unfolded substrate from Hsc70 to the substrate binding region of CCT. We also show that a similar interaction does not occur between their prokaryotic counterparts GroEL and DnaK, suggesting that in eukarya the two types of chaperones have evolved to a concerted action that makes the folding task more efficient.

journal_name

Nat Struct Mol Biol

authors

Cuéllar J,Martín-Benito J,Scheres SH,Sousa R,Moro F,López-Viñas E,Gómez-Puertas P,Muga A,Carrascosa JL,Valpuesta JM

doi

10.1038/nsmb.1464

subject

Has Abstract

pub_date

2008-08-01 00:00:00

pages

858-64

issue

8

eissn

1545-9993

issn

1545-9985

pii

nsmb.1464

journal_volume

15

pub_type

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