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TitleInter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateNov 4, 2020
AuthorsSara Alvira / Daniel W Watkins / Luca Troman / William J Allen / James S Lorriman / Gianluca Degliesposti / Eli J Cohen / Morgan Beeby / Bertram Daum / Vicki Am Gold / J Mark Skehel / Ian Collinson /
PubMed AbstractThe outer-membrane of Gram-negative bacteria is critical for surface adhesion, pathogenicity, antibiotic resistance and survival. The major constituent - hydrophobic β-barrel uter-embrane roteins ...The outer-membrane of Gram-negative bacteria is critical for surface adhesion, pathogenicity, antibiotic resistance and survival. The major constituent - hydrophobic β-barrel uter-embrane roteins (OMPs) - are first secreted across the inner-membrane through the Sec-translocon for delivery to periplasmic chaperones, for example SurA, which prevent aggregation. OMPs are then offloaded to the β-arrel ssembly achinery (BAM) in the outer-membrane for insertion and folding. We show the olo-ransocon (HTL) - an assembly of the protein-channel core-complex SecYEG, the ancillary sub-complex SecDF, and the membrane 'insertase' YidC - contacts BAM through periplasmic domains of SecDF and YidC, ensuring efficient OMP maturation. Furthermore, the proton-motive force (PMF) across the inner-membrane acts at distinct stages of protein secretion: (1) SecA-driven translocation through SecYEG and (2) communication of conformational changes via SecDF across the periplasm to BAM. The latter presumably drives efficient passage of OMPs. These interactions provide insights of inter-membrane organisation and communication, the importance of which is becoming increasingly apparent.
External linksElife / PubMed:33146611 / PubMed Central
MethodsEM (single particle)
Resolution18.23 Å
Structure data

EMDB-11240:
Cryo-EM structure of the E.coli HTL-BAm complex
Method: EM (single particle) / Resolution: 18.23 Å

Source
  • Escherichia coli (E. coli)

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