Stimulating the Substrate Folding Activity of a Single Ring GroEL Variant by Modulating the Cochaperonin GroES

被引：22

作者：

Illingworth, Melissa ^{[1
]}

Ramsey, Andrew ^{[1
]}

Zheng, Zhida ^{[1
]}

Chen, Lingling ^{[1
]}

机构：

[1] Indiana Univ, Dept Mol & Cellular Biochem, Bloomington, IN 47405 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2011年 / 286卷 / 35期

基金：

美国国家卫生研究院;

关键词：

PROTEIN-PROTEIN INTERACTIONS; CHAPERONIN GROEL; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; ATP HYDROLYSIS; OLIGOMERIC STRUCTURE; POLYPEPTIDE BINDING; IN-VIVO; CYCLE; MECHANISM;

D O I：

10.1074/jbc.M111.255935

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：

In mediating protein folding, chaperonin GroEL and cochaperonin GroES form an enclosed chamber for substrate proteins in an ATP-dependent manner. The essential role of the double ring assembly of GroEL is demonstrated by the functional deficiency of the single ring GroEL(SR). The GroEL(SR)-GroES is highly stable with minimal ATPase activity. To restore the ATP cycle and the turnover of the folding chamber, we sought to weaken the GroEL(SR)-GroES interaction systematically by concatenating seven copies of groES to generate groES(7). GroES Ile-25, Val-26, and Leu-27, residues on the GroEL-GroES interface, were substituted with Asp on different groES modules of groES(7). GroES(7) variants activate ATP activity of GroEL(SR), but only some restore the substrate folding function of GroEL(SR), indicating a direct role of GroES in facilitating substrate folding through its dynamics with GroEL. Active GroEL(SR)-GroES(7) systems may resemble mammalian mitochondrial chaperonin systems.

引用

页码：30401 / 30408

页数：8

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