Sinorhizobium meliloti Chemotaxis to Multiple Amino Acids Is Mediated by the Chemoreceptor McpU

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dc.contributor.authorWebb, Benjamin A.en
dc.contributor.authorCompton, K. Karlen
dc.contributor.authorDel Campo, Julia S. Martinen
dc.contributor.authorTaylor, Dorisen
dc.contributor.authorSobrado, Pabloen
dc.contributor.authorScharf, Birgit E.en
dc.contributor.departmentBiochemistryen
dc.contributor.departmentBiological Sciencesen
dc.contributor.departmentFralin Life Sciences Instituteen
dc.date.accessioned2017-12-18T20:01:35Zen
dc.date.available2017-12-18T20:01:35Zen
dc.date.issued2017-10-01en
dc.description.abstractSynthetic biology aims to design de novo biological systems and reengineer existing ones. These efforts have mostly focused on transcriptional circuits, with reengineering of signaling circuits hampered by limited understanding of their systems dynamics and experimental challenges. Bacterial two-component signaling systems offer a rich diversity of sensory systems that are built around a core phosphotransfer reaction between histidine kinases and their output response regulator proteins, and thus are a good target for reengineering through synthetic biology. Here, we explore the signalresponse relationship arising from a specific motif found in two-component signaling. In this motif, a single histidine kinase (HK) phosphotransfers reversibly to two separate output response regulator (RR) proteins. We show that, under the experimentally observed parameters from bacteria and yeast, this motif not only allows rapid signal termination, whereby one of the RRs acts as a phosphate sink towards the other RR (i.e. the output RR), but also implements a sigmoidal signalresponse relationship. We identify two mathematical conditions on system parameters that are necessary for sigmoidal signal-response relationships and define key parameters that control threshold levels and sensitivity of the signal-response curve. We confirm these findings experimentally, by in vitro reconstitution of the one HK-two RR motif found in the Sinorhizobium meliloti chemotaxis pathway and measuring the resulting signal-response curve. We find that the level of sigmoidality in this system can be experimentally controlled by the presence of the sink RR, and also through an auxiliary protein that is shown to bind to the HK (yielding Hill coefficients of above 7). These findings show that the one HK-two RR motif allows bacteria and yeast to implement tunable switch-like signal processing and provides an ideal basis for developing threshold devices for synthetic biology applications.en
dc.description.versionPublished versionen
dc.format.extent770 - 777 (8) page(s)en
dc.identifier.doihttps://doi.org/10.1094/MPMI-04-17-0096-Ren
dc.identifier.eissn1943-7706en
dc.identifier.issn0894-0282en
dc.identifier.issue10en
dc.identifier.orcidScharf, BE [0000-0001-6271-8972]en
dc.identifier.urihttp://hdl.handle.net/10919/81269en
dc.identifier.volume30en
dc.language.isoenen
dc.publisherAmer Phytopathological Socen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000410877000001&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.subjectBiotechnology & Applied Microbiologyen
dc.subjectPlant Sciencesen
dc.subjectRHIZOBIUM-MELILOTIen
dc.subjectBACTERIAL CHEMORECEPTORSen
dc.subjectBRADYRHIZOBIUM-JAPONICUMen
dc.subjectMOTILITYen
dc.subjectNODULATIONen
dc.subjectPLANTSen
dc.subjectLEGUMINOSARUMen
dc.subjectPROTEINSen
dc.subjectMUTANTSen
dc.subjectLEGUMESen
dc.titleSinorhizobium meliloti Chemotaxis to Multiple Amino Acids Is Mediated by the Chemoreceptor McpUen
dc.title.serialMolecular Plant-Microbe Interactionsen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
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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