@article{90541,
  keywords = {chemotaxis, Computer Simulation, Bacterial Proteins, Escherichia coli, Models, Biological, Escherichia coli Proteins, Adaptation, Physiological, Methyltransferases},
  author = {Clinton Hansen and Robert Endres and Ned Wingreen},
  title = {Chemotaxis in Escherichia coli: a molecular model for robust precise adaptation.},
  abstract = { The chemotaxis system in the bacterium Escherichia coli is remarkably sensitive to small relative changes in the concentrations of multiple chemical signals over a broad range of ambient concentrations. Interactions among receptors are crucial to this sensitivity as is precise adaptation, the return of chemoreceptor activity to prestimulus levels in a constant chemoeffector environment. Precise adaptation relies on methylation and demethylation of chemoreceptors by the enzymes CheR and CheB, respectively. Experiments indicate that when transiently bound to one receptor, these enzymes act on small assistance neighborhoods (AN) of five to seven receptor homodimers. In this paper, we model a strongly coupled complex of receptors including dynamic CheR and CheB acting on ANs. The model yields sensitive response and precise adaptation over several orders of magnitude of attractant concentrations and accounts for different responses to aspartate and serine. Within the model, we explore how the precision of adaptation is limited by small AN size as well as by CheR and CheB kinetics (including dwell times, saturation, and kinetic differences among modification sites) and how these kinetics contribute to noise in complex activity. The robustness of our dynamic model for precise adaptation is demonstrated by randomly varying biochemical parameters. },
  year = {2008},
  journal = {PLoS Comput Biol},
  volume = {4},
  pages = {e1},
  month = {01/2008},
  issn = {1553-7358},
  doi = {10.1371/journal.pcbi.0040001},
  language = {eng},
}