@article{87796,
  keywords = {Animals, chemotaxis, Bacterial Proteins, signal transduction, Escherichia coli, Structure-Activity Relationship, Chemoreceptor Cells, Receptors, Cell Surface, Escherichia coli Proteins},
  author = {Melinda Baker and Peter Wolanin and Jeffry Stock},
  title = {Signal transduction in bacterial chemotaxis.},
  abstract = { Motile bacteria respond to environmental cues to move to more favorable locations. The components of the chemotaxis signal transduction systems that mediate these responses are highly conserved among prokaryotes including both eubacterial and archael species. The best-studied system is that found in Escherichia coli. Attractant and repellant chemicals are sensed through their interactions with transmembrane chemoreceptor proteins that are localized in multimeric assemblies at one or both cell poles together with a histidine protein kinase, CheA, an SH3-like adaptor protein, CheW, and a phosphoprotein phosphatase, CheZ. These multimeric protein assemblies act to control the level of phosphorylation of a response regulator, CheY, which dictates flagellar motion. Bacterial chemotaxis is one of the most-understood signal transduction systems, and many biochemical and structural details of this system have been elucidated. This is an exciting field of study because the depth of knowledge now allows the detailed molecular mechanisms of transmembrane signaling and signal processing to be investigated. },
  year = {2006},
  journal = {Bioessays},
  volume = {28},
  pages = {9-22},
  month = {01/2006},
  issn = {0265-9247},
  doi = {10.1002/bies.20343},
  language = {eng},
}