"Push-pull networks, in which two antagonistic enzymes control the activity of a messenger protein, are ubiquitous in signal transduction pathways. A classical example is the chemotaxis system of the bacteriumEscherichia coli, in which the kinase CheA and the phosphatase CheZ regulate the phosphorylation level of themessenger protein CheY. Recent experiments suggest that both the kinase and the phosphatase are localized at the receptor cluster, and Vaknin and Berg recently demonstrated that the spatial distribution of the phosphatase can markedly affect the dose-response curves.We argue, using mathematical modeling, that the canonical model of the chemotaxis network cannot explain the experimental observations of Vaknin and Berg. We present a new model, in which a small fraction of the phosphatase is localized at the receptor cluster, while the remainder freely

Additional Metadata
Persistent URL dx.doi.org/10.1371/journal.pcbi.1000378
Journal PLoS Comput. Biol.
Citation
van Albada, S.B, & ten Wolde, P.R. (2009). Differential affinity and catalytic activity of CheZ in E. coli chemotaxis. PLoS Comput. Biol., 5(Article number: 1000378), 1–13. doi:10.1371/journal.pcbi.1000378