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dc.contributor.authorBryant, Owain J
dc.contributor.authorFraser, Gillian
dc.date.accessioned2021-12-22T15:07:15Z
dc.date.available2021-12-22T15:07:15Z
dc.date.issued2022-05
dc.date.submitted2021-03-23
dc.identifier.issn1742-464X
dc.identifier.otherfebs16294
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/331711
dc.description.abstractType III Secretion Systems (T3SS) transport proteins from the bacterial cytosol for assembly into cell surface nanomachines or direct delivery into target eukaryotic cells. At the core of the flagellar T3SS, the FlhAB-FliPQR export gate regulates protein entry into the export channel whilst maintaining the integrity of the cell membrane. Here, we identify critical residues in the export gate FliR plug that stabilise the closed conformation, preserving the membrane permeability barrier, and we show that the gate opens and closes in response to export substrate availability. Our data indicate that FlhAB-FliPQR gate opening, which is triggered by substrate export signals, is energised by FlhA in a proton motive force-dependent manner. We present evidence that the export substrate and the FliJ stalk of the flagellar ATPase provide mechanistically distinct, non-redundant gate-activating signals that are critical for efficient export.
dc.languageen
dc.publisherWiley
dc.subjectOriginal Article
dc.subjectOriginal Articles
dc.subjectbacterial flagella biogenesis
dc.subjectprotein export
dc.subjectType III secretion
dc.titleRegulation of bacterial Type III Secretion System export gate opening by substrates and the FliJ stalk of the flagellar ATPase.
dc.typeArticle
dc.date.updated2021-12-22T15:07:14Z
prism.publicationNameFEBS J
dc.identifier.doi10.17863/CAM.79161
dcterms.dateAccepted2021-11-22
rioxxterms.versionofrecord10.1111/febs.16294
rioxxterms.versionAO
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidFraser, Gillian [0000-0002-4874-8734]
dc.identifier.eissn1742-4658
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/M007197/1)
cam.issuedOnline2021-12-04


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