@article{90226,
  keywords = {Bacterial Proteins, signal transduction, Escherichia coli, Membrane Proteins, Flagella, Protein Multimerization, Methyl-Accepting Chemotaxis Proteins},
  author = {Anne-Florence Bitbol and Ned Wingreen},
  title = {Fundamental constraints on the abundances of chemotaxis proteins.},
  abstract = { Flagellated bacteria, such as Escherichia coli, perform directed motion in gradients of concentration of attractants and repellents in a process called chemotaxis. The E. coli chemotaxis signaling pathway is a model for signal transduction, but it has unique features. We demonstrate that the need for fast signaling necessitates high abundances of the proteins involved in this pathway. We show that further constraints on the abundances of chemotaxis proteins arise from the requirements of self-assembly both of flagellar motors and of chemoreceptor arrays. All these constraints are specific to chemotaxis, and published data confirm that chemotaxis proteins tend to be more highly expressed than their homologs in other pathways. Employing a chemotaxis pathway model, we show that the gain of the pathway at the level of the response regulator CheY increases with overall chemotaxis protein abundances. This may explain why, at least in one E. coli strain, the abundance of all chemotaxis proteins is higher in media with lower nutrient content. We also demonstrate that the E. coli chemotaxis pathway is particularly robust to abundance variations of the motor protein FliM. },
  year = {2015},
  journal = {Biophys J},
  volume = {108},
  pages = {1293-305},
  month = {03/2015},
  issn = {1542-0086},
  doi = {10.1016/j.bpj.2015.01.024},
  language = {eng},
}