From Chaperones to the Membrane with a BAM!

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• 作者：Ashlee M. Plummer¹ ; Karen G. Fleming¹ ; ^{Karen.Fleming@jhu.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：outer membrane proteins ; chaperones ; BAM complex
• 刊名：Trends in Biochemical Sciences
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：41
• 期：10
• 页码：872-882
• 全文大小：3404 K

文摘

Outer membrane proteins (OMPs) play a central role in the integrity of the outer membrane of Gram-negative bacteria. Unfolded OMPs (uOMPs) transit across the periplasm, and subsequent folding and assembly are crucial for biogenesis. Chaperones and the essential β-barrel assembly machinery (BAM) complex facilitate these processes. In vitro studies suggest that some chaperones sequester uOMPs in internal cavities during their periplasmic transit to prevent deleterious aggregation. Upon reaching the outer membrane, the BAM complex acts catalytically to accelerate uOMP folding. Complementary in vivo experiments have revealed the localization and activity of the BAM complex in living cells. Completing an understanding of OMP biogenesis will require a holistic view of the interplay among the individual components discussed here.