Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis
dc.contributor.author | Alvira, S | |
dc.contributor.author | Watkins, DW | |
dc.contributor.author | Troman, L | |
dc.contributor.author | Allen, WJ | |
dc.contributor.author | Lorriman, JS | |
dc.contributor.author | Degliesposti, G | |
dc.contributor.author | Cohen, EJ | |
dc.contributor.author | Beeby, M | |
dc.contributor.author | Daum, B | |
dc.contributor.author | Gold, VAM | |
dc.contributor.author | Skehel, JM | |
dc.contributor.author | Collinson, I | |
dc.date.accessioned | 2020-11-09T14:02:12Z | |
dc.date.issued | 2020-11-04 | |
dc.description.abstract | The outer-membrane of Gram-negative bacteria is critical for surface adhesion, pathogenicity, antibiotic resistance and survival. The major constituent – hydrophobic b-barrel Outer-Membrane Proteins (OMPs) – are first secreted across the inner-membrane through the Sec-translocon for delivery to periplasmic chaperones e.g. SurA, which prevent aggregation. OMPs are then offloaded to the b-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. | en_GB |
dc.description.sponsorship | European Commission | en_GB |
dc.identifier.citation | Vol. 9: e60669 | en_GB |
dc.identifier.doi | 10.7554/elife.60669 | |
dc.identifier.grantnumber | 803894 | en_GB |
dc.identifier.uri | http://hdl.handle.net/10871/123543 | |
dc.language.iso | en | en_GB |
dc.publisher | eLife Sciences Publications, Ltd | en_GB |
dc.rights | Licensed under a Creative Commons Attribution License. CC-BY 4.0 https://creativecommons.org/licenses/by/4.0/ | en_GB |
dc.title | Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2020-11-09T14:02:12Z | |
dc.identifier.issn | 2050-084X | |
dc.description | This is the author accepted manuscript. The final version is available from the publisher via the DOI in this record | en_GB |
dc.description | All data are available in the main text or the supplementary materials. The HTL-BAM cryo-EM structure has been deposited at the EMDB under the accession number 11240. | en_GB |
dc.identifier.journal | eLife | en_GB |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | en_GB |
dcterms.dateAccepted | 2020 | |
exeter.funder | ::European Commission | en_GB |
rioxxterms.version | AM | en_GB |
rioxxterms.licenseref.startdate | 2020-10-01 | |
rioxxterms.type | Journal Article/Review | en_GB |
refterms.dateFCD | 2020-11-09T13:57:08Z | |
refterms.versionFCD | AM | |
refterms.dateFOA | 2020-11-09T14:02:18Z | |
refterms.panel | A | en_GB |
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