1887

Abstract

We report the sequence and characterization of the gene. encodes a 61.8 kDa polypeptide (TlpC) which exhibits 30% amino acid identity with the methyl-accepting chemotaxis proteins (MCPs) and 38% identity with MCPs within the C-terminal domain. The putative methylation sites parallel those of the MCPs, rather than those of the receptors. TlpC is methylated both and although the level of methylation is poor. In addition, the anti-Trg antibody is shown to cross-react with this membrane protein. Inactivation of the gene confirms that TlpC is not one of the previously characterized MCPs from . Capillary assays were performed using a variety of chemoeffectors, which included all 20 amino acids, several sugars, and several compounds previously classified as repellents. However, no chemotactic defect was observed for any of the chemoeffectors tested. We suggest that TlpC is similar to an evolutionary intermediate from which the major chemotactic transducers from arose.

Loading

Article metrics loading...

/content/journal/micro/10.1099/13500872-140-8-1847
1994-08-01
2024-03-29
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/8/mic-140-8-1847.html?itemId=/content/journal/micro/10.1099/13500872-140-8-1847&mimeType=html&fmt=ahah

References

  1. Aim R.A., Manning P.A. Characterization of the hlyB gene and its role in the production of the El Tor haemolysin of Vibrio cholerae Ol. Mol Microbiol 1990; 4:413–425
    [Google Scholar]
  2. Alam M., Lebert M., Oesterhelt D., Hazelbauer G.L. Methyl-accepting chemotaxis proteins in Halobacterium halobium. EMBO J 1989; 8:631–639
    [Google Scholar]
  3. Alley M.R.K., Maddock J.R., Shapiro L. Polar localization of a bacterial chemoreceptor. Genes Dev 1992; 6:825–836
    [Google Scholar]
  4. Bedale W.A., Nettleton D.O., Sopata C.S., Thoelke M.S., Ordal G.W. Evidence for methyl-group transfer between the methyl-accepting chemotaxis proteins in Bacillus subtilis. J Bacteriol 1988; 170:223–227
    [Google Scholar]
  5. Bollinger J., Park C., Harayama S., Hazelbauer G.L. Structure of the Trg protein: homologies with and differences from other sensory transducers of Escherichia coli. Proc Natl Acad Sci USA 1984; 81:3287–3291
    [Google Scholar]
  6. Bourret R.B., Borkovich K.A., Simon M.I. Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Proc Natl Acad Sci USA 1990; 87:41–45
    [Google Scholar]
  7. Boyd A., Kendall K., Simon M.I. Structure of serine chemoreceptors in Escherichia coli. Nature 1983; 301:623–626
    [Google Scholar]
  8. Carpenter P.B., Hanlon D.W., Ordal G.W. flhE, a Bacillus subtilis flagellar gene that encodes a putative GTP-binding protein. Mol Microbiol 1992; 6:2705–2713
    [Google Scholar]
  9. Frederick K.L., Helmann J.D. Dual chemotaxis signaling pathways in Bacillus subtilis: a crD-dependent gene encodes a novel protein with both CheW and CheY homologous domains. J Bacteriol 1994; 176:2727–2735
    [Google Scholar]
  10. Goldman D.J., Ordal G.W. In vitro methylation and demethylation of methyl-accepting chemotaxis proteins in Bacillus subtilis. Biochemistry 1984; 23:2600–2606
    [Google Scholar]
  11. Goldman D.J., Worobec S.W., Siegel R.B., Hecker R.V., Ordal G.W. Chemotaxis in Bacillus subtilis: effects of attractants on the level of methylation of methyl-accepting chemotaxis proteins and the role of demethylation in the adaptation process. Biochemistry 1982; 21:915–920
    [Google Scholar]
  12. Hanahan D. Techniques for transformation of E coli. In DNA Cloning 1985 Edited by Glover D.M. Washington, DC: IRL Press; 1 pp 109–135
    [Google Scholar]
  13. Hanlon D.W., Ordal G.W. Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis. J Biol Chem 1994; 269:14038–14046
    [Google Scholar]
  14. Hanlon D.W., Ying C., Ordal G.W. Purification and characterization of methyl-accepting chemotaxis proteins from Bacillus subtilis. Biochim Biophys Acta 1993; 1158:345–351
    [Google Scholar]
  15. Hess J.F., Oosawa K., Kaplan N., Simon M.I. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell 1988; 53:79–87
    [Google Scholar]
  16. Kleene S.J., Toews M.L., Adler J. Isolation of a glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis. J Biol Chem 1977; 252:3214–3218
    [Google Scholar]
  17. Kort E.N., Goy M.F., Larsen S.H., Adler J. Methylation of a membrane protein involved in bacterial chemotaxis. Proc Natl Acad Sci USA 1975; 72:3939–3943
    [Google Scholar]
  18. Krikos A., Mutoh N., Boyd A., Simon M.I. Sensory transducers of Escherichia coli are composed of discrete structural and functional domains. Cell 1983; 33:615–622
    [Google Scholar]
  19. Lupas A., Stock J. Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. J Biol Chem 1989; 264:17337–17342
    [Google Scholar]
  20. Marquez L.M., Helmann J.D., Ferrari E.F., Parker H.M., Ordal G.W., Chamberlin M.J. Studies of a dependent functions in Bacillus subtilis. J Bacteriol 1990; 172:3435–3443
    [Google Scholar]
  21. McCleary W.R., Mcbride M.J., Zusman D.R. Developmental sensory transduction in Myxococcus xanthus involves methylation and demethylation of FrzCD. J Bacteriol 1990; 172:4877–4887
    [Google Scholar]
  22. Mirel D.B., Lustre V.M., Chamberlin M.J. An operon of Bacillus subtilis motility genes transcribed by the σD form of RNA polymerase. J Bacteriol 1992; 174:4197–4204
    [Google Scholar]
  23. Morgan D.G., Baumgartner J.W., Hazelbauer G.L. Proteins antigenically related to methyl-accepting chemotaxis proteins of Escherichia coli detected in a wide range of bacterial species. J Bacteriol 1993; 175:133–140
    [Google Scholar]
  24. Nowlin D.M., Nettleton D.O., Ordal G.W., Hazelbauer G.L. Chemotactic transducer proteins of Escherichia coli exh bit homology with methyl-accepting proteins from distantly related bacteria. J Bacteriol 1985; 163:262–266
    [Google Scholar]
  25. Ordal G.W., Goldman D.J. Chemotaxis away from uncouplers of oxidative phosphorylation in Bacillus subtilis. Science 1975; 189:802–805
    [Google Scholar]
  26. Ordal G.W., Goldman D.J. Chemotactic repellents of Bacillus subtilis. J Mol Biol 1976; 100:103–108
    [Google Scholar]
  27. Ordal G.W., Villani D.P., Gibson K.J. Amino acid chemoreceptors of Bacillus subtilis. J Bacteriol 1977; 129:156–165
    [Google Scholar]
  28. Ordal G.W., Villani D.P., Rosendahl M.S. Action of uncouplers of oxidative phosphorylation as chemotactic repellents of Bacillus subtilis. J Gen Microbiol 1979; 118:471–478
    [Google Scholar]
  29. Ordal G.W., Nettleton D.O., Hoch J.A. Genetics of Bacillus subtilis chemotaxis: isolation and mapping of mutants and cloning of chemotaxis genes. J Bacteriol 1983; 154:1088–1097
    [Google Scholar]
  30. Ordal G.W., Marquez-Magana L., Chamberlin M.J. Motility and chemotaxis. In Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry 1992 Edited by Sonenshein A.L. and others Washington, DC: American Society for Microbiology; Physiology, and Molecular Genetics, pp 765–784
    [Google Scholar]
  31. Rosario M.M.L., Frederick K.L., Ordal G.W., Helmann J.D. Chemotaxis in Bacillus subtilis requires either of two functionally redundant CheW homologs. J Bacteriol 1994; 176:2736–2739
    [Google Scholar]
  32. Rudner D.Z., Le Deaux J.R., Ireton K., Grossman A.D. The spoOK locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence. J Bacteriol 1991; 173:1388–1398
    [Google Scholar]
  33. Russo A.F., Koshland D.E. Jr Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing. Science 1983; 220:1016–1020
    [Google Scholar]
  34. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977; 74:5463–5467
    [Google Scholar]
  35. Stewart R.C., Roth A., Dahlquist F.W. Mutations that affect control of the methylesterase activity of CheB, a component of the chemotaxis adaptation system in Escherichia coli. J Bacteriol 1990; 172:3388–3399
    [Google Scholar]
  36. Tabor S., Richardson C.C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc Natl Acad Sci USA 1985; 82:1074–1078
    [Google Scholar]
  37. Taylor B.L., Lengeler J.W. Transductive coupling by methylated transducing proteins and permeases of the phosphotransferase system in bacterial chemotaxis. In Membrane Transport and Information Storage 1990 Edited by Aloia R.C. New York: Alan R. Liss; pp 69–90
    [Google Scholar]
  38. Ullah A.J.H., Ordal G.W. In vivo and in vitro chemotactic methylation in Bacillus subtilis. J Bacteriol 1981; 145:958–965
    [Google Scholar]
  39. Van der Werf P., Koshland D.E. Jr Identification of a y-glutamyl methyl ester in bacterial membrane protein involved in chemotaxis. J Biol Chem 1977; 252:2793–2795
    [Google Scholar]
  40. Vellanoweth R.L., Rabinowitz J.C. The influence of ribosome-binding-site elements on translational efficiency in Bacillus subtilis and Escherichia coli in vivo. Mol Microbiol 1992; 6:1105–1114
    [Google Scholar]
  41. Vosman B., Kuiken G., Kooistra J., Venema G. Transformation in Bacillus subtilis: involvement of the 17-kilodalton DNA-entry nuclease and the competence specific 18-kilodalton protein. J Bacteriol 1988; 170:3703–3710
    [Google Scholar]
  42. Yao V.J., Spudich J.L. Primary structure of an archaebacterial transducer, a methyl-acepting protein associated with sensory rhodopsin I. Proc Natl Acad Sci USA 1993; 89:11915–11919
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-140-8-1847
Loading
/content/journal/micro/10.1099/13500872-140-8-1847
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error