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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.

Original publication




Journal article


Prog Biophys Mol Biol

Publication Date





40 - 46


Bacterial Proteins, Chemotaxis, Escherichia coli, Gene Expression Regulation, Bacterial, Membrane Proteins, Methyl-Accepting Chemotaxis Proteins, Models, Biological, Phosphorylation, Time Factors