Membrane protein architects: the role of the BAM complex in outer membrane protein assembly

被引：278

作者：

Knowles, Timothy J. ^{[2
]}

Scott-Tucker, Anthony ^{[1
]}

Overduin, Michael ^{[2
]}

Henderson, Ian R. ^{[1
]}

机构：

[1] Univ Birmingham, Div Immun & Infect, Birmingham B15 2TT, W Midlands, England

[2] Univ Birmingham, Canc Res UK Inst Canc Studies, Sch Canc Sci, Birmingham B15 2TT, W Midlands, England

来源：

NATURE REVIEWS MICROBIOLOGY | 2009年 / 7卷 / 03期

基金：

英国医学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

BETA-BARREL PROTEINS; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; BACTERIAL PROTEIN; CYTOPLASMIC MEMBRANE; FUNCTIONAL DOMAINS; CHAPERONE ACTIVITY; SECRETIN PULD; LIPID EXPORT; YAET COMPLEX;

D O I：

10.1038/nrmicro2069

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The folding of transmembrane proteins into the outer membrane presents formidable challenges to Gram-negative bacteria. These proteins must migrate from the cytoplasm, through the inner membrane and into the periplasm, before being recognized by the beta-barrel assembly machinery, which mediates efficient insertion of folded beta-barrels into the outer membrane. Recent discoveries of component structures and accessory interactions of this complex are yielding insights into how cells fold membrane proteins. Here, we discuss how these structures illuminate the mechanisms responsible for the biogenesis of outer membrane proteins.

引用

页码：206 / 214

页数：9

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