Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis
The outer-membrane of Gram-negative bacteria is critical for surface adhesion, pathogenicity, antibiotic resistance and survival. The major constituent – hydrophobic β-barrel Outer-Membrane Proteins (OMPs) – are first secreted across the inner-membrane through the Sec-translocon for delivery to peri...
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doaj-f24b1cd117cb40268b4bfbcedb0b00c82021-05-05T21:40:59ZengeLife Sciences Publications LtdeLife2050-084X2020-11-01910.7554/eLife.60669Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesisSara Alvira0Daniel W Watkins1https://orcid.org/0000-0003-3825-5036Lucy Troman2William J Allen3https://orcid.org/0000-0002-9513-4786James S Lorriman4https://orcid.org/0000-0002-1755-0805Gianluca Degliesposti5Eli J Cohen6Morgan Beeby7https://orcid.org/0000-0001-6413-9835Bertram Daum8https://orcid.org/0000-0002-3767-264XVicki AM Gold9https://orcid.org/0000-0002-6908-0745J Mark Skehel10Ian Collinson11https://orcid.org/0000-0002-3931-0503School of Biochemistry, University of Bristol, Bristol, United KingdomSchool of Biochemistry, University of Bristol, Bristol, United KingdomSchool of Biochemistry, University of Bristol, Bristol, United KingdomSchool of Biochemistry, University of Bristol, Bristol, United KingdomSchool of Biochemistry, University of Bristol, Bristol, United KingdomBiological Mass Spectrometry and Proteomics, MRC Laboratory of Molecular Biology, Cambridge, United KingdomDepartment of Life Sciences, Imperial College London, London, United KingdomDepartment of Life Sciences, Imperial College London, London, United KingdomLiving Systems Institute, University of Exeter, Exeter, United Kingdom; College of Life and Environmental Sciences, University of Exeter, Exeter, United KingdomLiving Systems Institute, University of Exeter, Exeter, United Kingdom; College of Life and Environmental Sciences, University of Exeter, Exeter, United KingdomBiological Mass Spectrometry and Proteomics, MRC Laboratory of Molecular Biology, Cambridge, United KingdomSchool of Biochemistry, University of Bristol, Bristol, United KingdomThe outer-membrane of Gram-negative bacteria is critical for surface adhesion, pathogenicity, antibiotic resistance and survival. The major constituent – hydrophobic β-barrel Outer-Membrane Proteins (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-Barrel Assembly Machinery (BAM) in the outer-membrane for insertion and folding. We show the Holo-TransLocon (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.https://elifesciences.org/articles/60669BAM complexsec complexholotransloconouter membrane proteinHTL-BAMSecYEG |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sara Alvira Daniel W Watkins Lucy Troman William J Allen James S Lorriman Gianluca Degliesposti Eli J Cohen Morgan Beeby Bertram Daum Vicki AM Gold J Mark Skehel Ian Collinson |
spellingShingle |
Sara Alvira Daniel W Watkins Lucy Troman William J Allen James S Lorriman Gianluca Degliesposti Eli J Cohen Morgan Beeby Bertram Daum Vicki AM Gold J Mark Skehel Ian Collinson Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis eLife BAM complex sec complex holotranslocon outer membrane protein HTL-BAM SecYEG |
author_facet |
Sara Alvira Daniel W Watkins Lucy Troman William J Allen James S Lorriman Gianluca Degliesposti Eli J Cohen Morgan Beeby Bertram Daum Vicki AM Gold J Mark Skehel Ian Collinson |
author_sort |
Sara Alvira |
title |
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis |
title_short |
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis |
title_full |
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis |
title_fullStr |
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis |
title_full_unstemmed |
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis |
title_sort |
inter-membrane association of the sec and bam translocons for bacterial outer-membrane biogenesis |
publisher |
eLife Sciences Publications Ltd |
series |
eLife |
issn |
2050-084X |
publishDate |
2020-11-01 |
description |
The outer-membrane of Gram-negative bacteria is critical for surface adhesion, pathogenicity, antibiotic resistance and survival. The major constituent – hydrophobic β-barrel Outer-Membrane Proteins (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-Barrel Assembly Machinery (BAM) in the outer-membrane for insertion and folding. We show the Holo-TransLocon (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. |
topic |
BAM complex sec complex holotranslocon outer membrane protein HTL-BAM SecYEG |
url |
https://elifesciences.org/articles/60669 |
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