Spatiotemporal modelling of CheY complexes in Escherichia coli chemotaxis.
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.
Tindall
M J
MJ
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
Porter
S L
SL
Wadhams
G H
GH
Maini
P K
PK
Armitage
J P
JP
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
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607606:cheY protein, E coli