Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 41, Issue 10, Pages 872-882Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2016.06.005
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Funding
- NIGMS NIH HHS [R01 GM079440, T32 GM008403] Funding Source: Medline
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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 D-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.
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