Journal
NATURE REVIEWS MICROBIOLOGY
Volume 7, Issue 3, Pages 206-214Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nrmicro2069
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Funding
- Biotechnology and Biological Sciences Research Council [BB/F000472/1, BB/G022054/1] Funding Source: Medline
- Medical Research Council [G0700151] Funding Source: Medline
- BBSRC [BB/F000472/1, BB/G022054/1] Funding Source: UKRI
- MRC [G0700151] Funding Source: UKRI
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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.
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