BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism

被引:29
作者
Plummer, Ashlee M. [1 ]
Fleming, Karen G. [1 ]
机构
[1] Johns Hopkins Univ, Thomas C Jenkins Dept Biophys, Baltimore, MD 21218 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
ESCHERICHIA-COLI; DODECYL-SULFATE; YAET COMPLEX; BIOGENESIS; CONFORMATION;
D O I
10.1021/acs.biochem.5b00950
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
beta-Barrel assembly machinery protein A (BamA) plays a critical role in the biogenesis of outer membrane proteins (OMPs); however, a mechanistic understanding of its function is lacking. Here, we report an in vitro assay that investigates whether the mechanism of BamA-catalyzed OMP folding is stoichiometric or catalytic. We found that BamA accelerates the folding of OMPs in vitro via a catalytic mechanism, similar to the activity of the full multiprotein beta-barrel assembly machinery (BAM) complex in vivo. As BamA alone can repeatedly facilitate the folding of OMPs, we suggest the additional BAM components accelerate this basal activity to biologically relevant time scales.
引用
收藏
页码:6009 / 6011
页数:3
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