title: Chemotactic signal integration in bacteria.
abstract: Chemotactic signaling in Escherichia coli involves transmission of both negative and positive signals. In order to examine mechanisms of signal processing, behavioral responses to dual inputs have been measured by using photoactivable "caged" compounds, computer video analysis, and chemoreceptor deletion mutants. Signaling from Tar and Tsr, two receptors that sense amino acids and pH, was studied. In a Tar deletion mutant the photoactivated release of protons, a Tsr repellent, and of serine, a Tsr attractant, in separate experiments at pH 7.0 resulted in tumbling (negative) or smooth-swimming (positive) responses in ca. 50 and 140 ms, respectively. Simultaneous photorelease of protons and serine resulted in a single tumbling or smooth-swimming response, depending on the relative amounts of the two effectors. In contrast, in wild-type E. coli, proton release at pH 7.0 resulted in a biphasic response that was attributed to Tsr-mediated tumbling followed by Tar-mediated smooth-swimming. In wild-type E. coli at more alkaline pH values the Tar-mediated signal was stronger than the Tsr signal, resulting in a strong smooth-swimming response preceded by a diminished tumbling response. These observations imply that (i) a single receptor time-averages the binding of different chemotactic ligands generating a single response; (ii) ligand binding to different receptors can result in a nonintegrated response with the tumbling response preceding the smooth-swimming response; (iii) however, chemotactic signals of different intensities derived from different receptors can also result in an apparently integrated response; and (iv) the different chemotactic responses to protons at neutral and alkaline pH may contribute to E. coli migration toward neutrality.
authors.affiliation: Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
authors.forename: S
authors.initials: S
authors.lastname: Khan
authors.forename: J L
authors.initials: JL
authors.lastname: Spudich
authors.forename: J A
authors.initials: JA
authors.lastname: McCray
authors.forename: D R
authors.initials: DR
authors.lastname: Trentham
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002628:Chemoreceptor Cells; D002633:Chemotaxis / Q000502:physiology*; D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D018715:Microscopy, Video; D008954:Models, Biological; D010755:Organophosphates / Q000378:metabolism; D011522:Protons; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D012694:Serine / Q000031:analogs & derivatives / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008024:Ligands; D008565:Membrane Proteins; D010755:Organophosphates; D011522:Protons; D011956:Receptors, Cell Surface; C057331:Tar protein, E coli; C057635:Tsr protein, Bacteria; C085918:N-1-(2-nitrophenyl)ethoxycarbonylserine; C085919:2-hydroxyphenyl 1-(2-nitrophenyl)ethyl phosphate; D012694:Serine