Show simple item record

dc.contributor.authorTindall, MJ
dc.contributor.authorPorter, SL
dc.contributor.authorMaini, PK
dc.contributor.authorArmitage, JP
dc.date.accessioned2013-06-03T09:17:29Z
dc.date.issued2010
dc.description.abstractUnderstanding how multiple signals are integrated in living cells to produce a balanced response is a major challenge in biology. Two-component signal transduction pathways, such as bacterial chemotaxis, comprise histidine protein kinases (HPKs) and response regulators (RRs). These are used to sense and respond to changes in the environment. Rhodobacter sphaeroides has a complex chemosensory network with two signaling clusters, each containing a HPK, CheA. Here we demonstrate, using a mathematical model, how the outputs of the two signaling clusters may be integrated. We use our mathematical model supported by experimental data to predict that: (1) the main RR controlling flagellar rotation, CheY(6), aided by its specific phosphatase, the bifunctional kinase CheA(3), acts as a phosphate sink for the other RRs; and (2) a phosphorelay pathway involving CheB(2) connects the cytoplasmic cluster kinase CheA(3) with the polar localised kinase CheA(2), and allows CheA(3)-P to phosphorylate non-cognate chemotaxis RRs. These two mechanisms enable the bifunctional kinase/phosphatase activity of CheA(3) to integrate and tune the sensory output of each signaling cluster to produce a balanced response. The signal integration mechanisms identified here may be widely used by other bacteria, since like R. sphaeroides, over 50% of chemotactic bacteria have multiple cheA homologues and need to integrate signals from different sources.en_GB
dc.identifier.citationPLoS Computational Biology, 2010, Vol. 6, Issue 8en_GB
dc.identifier.doi10.1371/journal.pcbi.1000896
dc.identifier.urihttp://hdl.handle.net/10871/9782
dc.language.isoenen_GB
dc.publisherPublic Library of Scienceen_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/20808885en_GB
dc.subjectBacterial Proteinsen_GB
dc.subjectChemotaxisen_GB
dc.subjectFlagellaen_GB
dc.subjectMembrane Proteinsen_GB
dc.subjectModels, Biologicalen_GB
dc.subjectPhosphoric Monoester Hydrolasesen_GB
dc.subjectPhosphorylationen_GB
dc.subjectProtein Kinasesen_GB
dc.subjectRhodobacter sphaeroidesen_GB
dc.subjectSignal Transductionen_GB
dc.titleModeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase.en_GB
dc.typeArticleen_GB
dc.date.available2013-06-03T09:17:29Z
exeter.place-of-publicationUnited States
dc.descriptionaddresses: Centre for Mathematical Biology, Mathematical Institute, University of Oxford, Oxford, United Kingdom. m.tindall@reading.ac.uken_GB
dc.descriptionnotes: PMCID: PMC2924250en_GB
dc.descriptiontypes: Journal Article; Research Support, Non-U.S. Gov'ten_GB
dc.descriptionCopyright: © 2010 Tindall et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_GB
dc.identifier.journalPLoS Computational Biologyen_GB


Files in this item

This item appears in the following Collection(s)

Show simple item record