title: Spatiotemporal modelling of CheY complexes in Escherichia coli chemotaxis.
abstract: The chemotaxis pathway of Escherichia coli is one of the best studied and modelled biological signalling pathways. Here we extend existing modelling approaches by explicitly including a description of the formation and subcellular localization of intermediary complexes in the phosphotransfer pathway. The inclusion of these complexes shows that only about 60% of the total output response regulator (CheY) is uncomplexed at any moment and hence free to interact with its target, the flagellar motor. A clear strength of this model is its ability to predict the experimentally observable subcellular localization of CheY throughout a chemotactic response. We have found good agreement between the model output and experimentally determined CheY localization patterns.
authors.affiliation: Institute for Cardiovascular and Metabolic Research and School of Biological Sciences and Department of Mathematics, University of Reading, Whiteknights, Reading, Berkshire RG6 6AP, UK. m.tindall@reading.ac.uk
authors.forename: M J
authors.initials: MJ
authors.lastname: Tindall
authors.forename: S L
authors.initials: SL
authors.lastname: Porter
authors.forename: G H
authors.initials: GH
authors.lastname: Wadhams
authors.forename: P K
authors.initials: PK
authors.lastname: Maini
authors.forename: J P
authors.initials: JP
authors.lastname: Armitage
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D002633:Chemotaxis; D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D008565:Membrane Proteins / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008954:Models, Biological; D010766:Phosphorylation; D013997:Time Factors
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607606:cheY protein, E coli