The structure of CCT-Hsc70NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin

被引：70

作者：

Cuellar, Jorge ^{[1
]}

Martin-Benito, Jaime ^{[1
]}

Scheres, Sjors H. W. ^{[1
]}

Sousa, Rui ^{[2
]}

Moro, Fernando ^{[3
]}

Lopez-Vinas, Eduardo ^{[4
,5
]}

Gomez-Puertas, Paulino ^{[4
]}

Muga, Arturo ^{[3
]}

Carrascosa, Jose L. ^{[1
]}

Valpuesta, Jose M. ^{[1
]}

机构：

[1] CSIC, Ctr Nacl Biotecnol, Madrid 28049, Spain

[2] Univ Texas Hlth Sci Ctr San Antonio, Dept Biochem, San Antonio, TX 78229 USA

[3] Univ Basque Country, Dept Bioquim & Biol Mol, E-48080 Bilbao, Spain

[4] UAM, CSIC, Ctr Biol Mol Serv Ochoa, Madrid 28049, Spain

[5] ISCIII, CIBER Physiopathol Obes & Nutr CB06 03 0026, Madrid, Spain

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 08期

关键词：

D O I：

10.1038/nsmb.1464

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 CCTb 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.

引用

页码：858 / 864

页数：7

共 49 条

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