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Regulation of bacterial Type III Secretion System export gate opening by substrates and the FliJ stalk of the flagellar ATPase.

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cam.issuedOnline2021-12-04
dc.contributor.authorBryant, Owain J
dc.contributor.authorFraser, Gillian M
dc.contributor.orcidFraser, Gillian M [0000-0002-4874-8734]
dc.date.accessioned2021-12-22T15:07:15Z
dc.date.available2021-12-22T15:07:15Z
dc.date.issued2022-05
dc.date.submitted2021-03-23
dc.date.updated2021-12-22T15:07:14Z
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.identifier.doi10.17863/CAM.79161
dc.identifier.eissn1742-4658
dc.identifier.issn1742-464X
dc.identifier.otherfebs16294
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/331711
dc.languageen
dc.language.isoeng
dc.publisherWiley
dc.publisher.urlhttp://dx.doi.org/10.1111/febs.16294
dc.subjectType III secretion
dc.subjectbacterial flagella biogenesis
dc.subjectprotein export
dc.subjectAdenosine Triphosphatases
dc.subjectBacteria
dc.subjectBacterial Proteins
dc.subjectFlagella
dc.subjectProtein Transport
dc.subjectType III Secretion Systems
dc.titleRegulation of bacterial Type III Secretion System export gate opening by substrates and the FliJ stalk of the flagellar ATPase.
dc.typeArticle
dcterms.dateAccepted2021-11-22
prism.publicationNameFEBS J
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/M007197/1)
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1111/febs.16294

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