Sinorhizobium meliloti chemotaxis to quaternary ammonium compounds is mediated by the chemoreceptor McpX

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dc.contributor.authorWebb, Benjamin A.en
dc.contributor.authorCompton, K. Karlen
dc.contributor.authorSaldaña, Rafael Castañedaen
dc.contributor.authorArapov, Timofey D.en
dc.contributor.authorRay, W. Keithen
dc.contributor.authorHelm, Richard F.en
dc.contributor.authorScharf, Birgit E.en
dc.contributor.departmentBiochemistryen
dc.contributor.departmentBiological Sciencesen
dc.date.accessioned2017-12-18T20:15:05Zen
dc.date.available2017-12-18T20:15:05Zen
dc.date.issued2017-01-01en
dc.description.abstractThe bacterium Sinorhizobium meliloti is attracted to seed exudates of its host plant alfalfa <i>(Medicago sativa).</i> Since quaternary ammonium compounds (QACs) are exuded by germinating seeds, we assayed chemotaxis of S. meliloti towards betonicine, choline, glycine betaine, stachydrine and trigonelline. The wild type displayed a positive response to all QACs. Using LC–MS, we determined that each germinating alfalfa seed exuded QACs in the nanogram range. Compared to the closely related nonhost species, spotted medic <i>(Medicago arabica),</i> unique profiles were released. Further assessments of single chemoreceptor deletion strains revealed that an mcpX deletion strain displayed little to no response to these compounds. Differential scanning fluorimetry showed interaction of the isolated periplasmic region of McpX (McpX<sup>PR</sup> and McpX<sub>34-306</sub>) with QACs. Isothermal titration calorimetry experiments revealed tight binding to McpX<sup>PR</sup> with dissociation constants (K<sub>d</sub>) in the nanomolar range for choline and glycine betaine, micromolar K<sub>d</sub> for stachydrine and trigonelline and a K<sub>d</sub> in the millimolar range for betonicine. Our discovery of <i>S. meliloti</i> chemotaxis to plantderived QACs adds another role to this group of compounds, which are known to serve as nutrient sources, osmoprotectants and cell-to-cell signalling molecules. This is the first report of a chemoreceptor that mediates QACs taxis through direct binding.en
dc.description.versionPublished versionen
dc.format.extent333 - 346 (14) page(s)en
dc.identifier.doihttps://doi.org/10.1111/mmi.13561en
dc.identifier.eissn1365-2958en
dc.identifier.issn0950-382Xen
dc.identifier.issue2en
dc.identifier.orcidHelm, RF [0000-0001-5317-0925]en
dc.identifier.orcidScharf, BE [0000-0001-6271-8972]en
dc.identifier.urihttp://hdl.handle.net/10919/81270en
dc.identifier.volume103en
dc.language.isoenen
dc.publisherWiley-Blackwellen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000394691500012&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectBiochemistry & Molecular Biologyen
dc.subjectMicrobiologyen
dc.subjectTANDEM MASS-SPECTROMETRYen
dc.subjectRHIZOBIUM-MELILOTIen
dc.subjectGLYCINE BETAINEen
dc.subjectAMINO-ACIDSen
dc.subjectESCHERICHIA-COLIen
dc.subjectPROLINE BETAINEen
dc.subjectBRADYRHIZOBIUM-JAPONICUMen
dc.subjectSALT TOLERANCEen
dc.subjectHUMAN-URINEen
dc.subjectBACTERIAen
dc.titleSinorhizobium meliloti chemotaxis to quaternary ammonium compounds is mediated by the chemoreceptor McpXen
dc.title.serialMolecular Microbiologyen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biochemistryen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
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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