@article{90521,
  keywords = {Fluorescence Resonance Energy Transfer, Aspartic Acid, Principal Component Analysis, chemotaxis, Computer Simulation, Bacterial Proteins, signal transduction, Escherichia coli, Models, Biological, Chemoreceptor Cells, Membrane Proteins, Ligands, Recombinant Fusion Proteins, Receptors, Cell Surface, Escherichia coli Proteins, Reproducibility of Results, Methyltransferases, Methyl-Accepting Chemotaxis Proteins},
  author = {Robert Endres and Olga Oleksiuk and Clinton Hansen and Yigal Meir and Victor Sourjik and Ned Wingreen},
  title = {Variable sizes of Escherichia coli chemoreceptor signaling teams.},
  abstract = { Like many sensory receptors, bacterial chemotaxis receptors form clusters. In bacteria, large-scale clusters are subdivided into signaling teams that act as {\textquoteright}antennas{\textquoteright} allowing detection of ligands with remarkable sensitivity. The range of sensitivity is greatly extended by adaptation of receptors to changes in concentrations through covalent modification. However, surprisingly little is known about the sizes of receptor signaling teams. Here, we combine measurements of the signaling response, obtained from in vivo fluorescence resonance energy transfer, with the statistical method of principal component analysis, to quantify the size of signaling teams within the framework of the previously successful Monod-Wyman-Changeux model. We find that size of signaling teams increases 2- to 3-fold with receptor modification, indicating an additional, previously unrecognized level of adaptation of the chemotaxis network. This variation of signaling-team size shows that receptor cooperativity is dynamic and likely optimized for sensing noisy ligand concentrations. },
  year = {2008},
  journal = {Mol Syst Biol},
  volume = {4},
  pages = {211},
  issn = {1744-4292},
  doi = {10.1038/msb.2008.49},
  language = {eng},
}