The type IV pilus assembly ATPase PilB functions as a signaling protein to regulate exopolysaccharide production in Myxococcus xanthus

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dc.contributor.authorBlack, Wesley P.en
dc.contributor.authorWang, Linglingen
dc.contributor.authorJing, Xingen
dc.contributor.authorSaldaña, Rafael Castañedaen
dc.contributor.authorLi, Fengen
dc.contributor.authorScharf, Birgit E.en
dc.contributor.authorSchubot, Florian D.en
dc.contributor.authorYang, Zhaominen
dc.contributor.departmentBiological Sciencesen
dc.date.accessioned2017-12-18T18:38:01Zen
dc.date.available2017-12-18T18:38:01Zen
dc.date.issued2017-08-04en
dc.description.abstractMyxococcus xanthus possesses a form of surface motility powered by the retraction of the type IV pilus (T4P). Additionally, exopolysaccharide (EPS), the major constituent of bacterial biofilms, is required for this T4P-mediated motility in M. xanthus as the putative trigger of T4P retraction. The results here demonstrate that the T4P assembly ATPase PilB functions as an intermediary in the EPS regulatory pathway composed of the T4P upstream of the Dif signaling proteins in M. xanthus. A suppressor screen isolated a pilB mutation that restored EPS production to a T4P− mutant. An additional PilB mutant variant, which is deficient in ATP hydrolysis and T4P assembly, supports EPS production without the T4P, indicating PilB can regulate EPS production independently of its function in T4P assembly. Further analysis confirms that PilB functions downstream of the T4P filament but upstream of the Dif proteins. In vitro studies suggest that the nucleotide-free form of PilB assumes the active signaling conformation in EPS regulation. Since M. xanthus PilB possesses conserved motifs with high affinity for c-di-GMP binding, the findings here suggest that c-di-GMP can regulate both motility and biofilm formation through a single effector in this surface-motile bacterium.en
dc.description.versionPublished versionen
dc.format.extent? - ? (13) page(s)en
dc.identifier.doihttps://doi.org/10.1038/s41598-017-07594-xen
dc.identifier.issn2045-2322en
dc.identifier.orcidScharf, BE [0000-0001-6271-8972]en
dc.identifier.orcidYang, Z [0000-0002-2044-6793]en
dc.identifier.urihttp://hdl.handle.net/10919/81268en
dc.identifier.volume7en
dc.languageEnglishen
dc.publisherNature Publishing Groupen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000406980800002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectsocial gliding motilityen
dc.subjectcyclic di-gmpen
dc.subjectfocal adhesion complexesen
dc.subjectmolecular-mechanismen
dc.subjectchemotaxis homologsen
dc.subjectcell-interactionsen
dc.subjectmyxobacteriaen
dc.subjectretractionen
dc.subjectinsightsen
dc.subjectbacteriaen
dc.titleThe type IV pilus assembly ATPase PilB functions as a signaling protein to regulate exopolysaccharide production in Myxococcus xanthusen
dc.title.serialScientific Reportsen
dc.typeArticle - Refereeden
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/Scienceen
pubs.organisational-group/Virginia Tech/Science/Biological Sciencesen
pubs.organisational-group/Virginia Tech/Science/COS T&R Facultyen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciencesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciences/Fralin Affiliated Facultyen

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