FliL and its paralog MotF have distinct roles in the stator activity of the Sinorhizobium meliloti flagellar motor

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dc.contributor.authorSobe, Richard C.en
dc.contributor.authorGilbert, Crystalen
dc.contributor.authorVo, Lamen
dc.contributor.authorAlexandre, Gladysen
dc.contributor.authorScharf, Birgit E.en
dc.date.accessioned2024-01-22T14:26:39Zen
dc.date.available2024-01-22T14:26:39Zen
dc.date.issued2022-07-28en
dc.description.abstractThe bacterial flagellum is a complex macromolecular machine that drives bacteria through diverse fluid environments. Although many components of the flagellar motor are conserved across species, the roles of FliL are numerous and species-specific. Here, we have characterized an additional player required for flagellar motor function in Sinorhizobium meliloti, MotF, which we have identified as a FliL paralog. We performed a comparative analysis of MotF and FliL, identified interaction partners through bacterial two-hybrid and pull-down assays, and investigated their roles in motility and motor rotation. Both proteins form homooligomers, and interact with each other, and with the stator proteins MotA and MotB. The ∆motF mutant exhibits normal flagellation but its swimming behavior and flagellar motor activity are severely impaired and erratic. In contrast, the ∆fliL mutant is mostly aflagellate and nonmotile. Amino acid substitutions in cytoplasmic regions of MotA or disruption of the proton channel plug of MotB partially restored motor activity to the ∆motF but not the ∆fliL mutant. Altogether, our findings indicate that both, MotF and FliL, are essential for flagellar motor torque generation in S. meliloti. FliL may serve as a scaffold for stator integration into the motor, and MotF is required for proton channel modulation.en
dc.description.versionPublished versionen
dc.format.extentPages 223-243en
dc.format.extent21 page(s)en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1111/mmi.14964en
dc.identifier.eissn1365-2958en
dc.identifier.issn0950-382Xen
dc.identifier.issue3en
dc.identifier.orcidScharf, Birgit [0000-0001-6271-8972]en
dc.identifier.pmid35808893en
dc.identifier.urihttps://hdl.handle.net/10919/117508en
dc.identifier.volume118en
dc.language.isoenen
dc.publisherWileyen
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/35808893en
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.subjectchemotaxisen
dc.subjectflagellar-basal bodyen
dc.subjectproton channel plugen
dc.subjectswimming motilityen
dc.subjecttorque generationen
dc.subject.meshFlagellaen
dc.subject.meshSinorhizobium melilotien
dc.subject.meshProtonsen
dc.subject.meshBacterial Proteinsen
dc.subject.meshTorqueen
dc.subject.meshMolecular Motor Proteinsen
dc.titleFliL and its paralog MotF have distinct roles in the stator activity of the <i>Sinorhizobium meliloti</i> flagellar motoren
dc.title.serialMolecular Microbiologyen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherArticleen
dc.type.otherJournalen
dcterms.dateAccepted2022-07-06en
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Scienceen
pubs.organisational-group/Virginia Tech/Science/Biological Sciencesen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Science/COS T&R Facultyen

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