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Gene Review

tsr  -  methyl-accepting chemotaxis protein I,...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4345, JW4318, cheD
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Disease relevance of tsr

  • We present here the nucleotide sequence of the tsr gene of E. coli; the amino acid sequence derived from it suggests that the Tsr transducer protein has a relatively simple transmembrane structure that may place limits on the mechanisms available for the transmission of sensory information into the cell [1].
  • Synthesis of the tsr and tar products was directed in ultraviolet-irradiated bacteria by lambda transducing phages [2].
  • We demonstrate here that the expression of the Escherichia coli chemoreceptor gene tsr, with 2.6 kilobases of its upstream sequence, is temporally controlled in Caulobacter crescentus [3].
  • Streptomyces viridochromogenes was transformed by single stranded DNA integration vectors in order to replace the pat by the tsr gene and generate mutants unable to synthesize phosphinothricin-tripeptide (PTT) [4].
  • We characterized mutants in two novel genes of Bacillus subtilis, cheC and cheD [5].

High impact information on tsr


Chemical compound and disease context of tsr


Biological context of tsr

  • Correlation of this protein sequence data with the nucleotide sequence of the tsr gene [Boyd, A., Kendall, K. & Simon, M.I. (1983) Nature (London) 301, 623-626] suggests that CheB-dependent modification of MCPI is the enzymatic deamidation of glutamine to methyl-accepting glutamic acid [13].
  • We then introduced either an aer or tsr mutation into each mutant to create two sets of electron transport mutants [14].
  • Strain HCB326 (cheAWRBYZ tar tap tsr trg::Tn10), which was deficient in all chemotaxis components except the switch and motor, was transformed with the pCK63 plasmid (ptac-cheY+) [15].
  • The conclusion that methylation generates multiplicity was supported by the results of experiments in which the tsr product was synthesized in mutant bacteria defective in specific chemotaxis functions concerned with methylation or demethylation of MCPs [2].
  • The apparent transcription start site of the E. coli tsr gene was determined in both E. coli and C. crescentus, and we found that in both backgrounds the promoter used conforms to the consensus sequence for the promoters of the flagellar and chemosensory genes of Bacillus subtilis and E. coli [3].

Anatomical context of tsr

  • The prevalence and function of four chemoreceptors, Tsr, Tar, Trg, and Tap, were determined for a collection of uropathogenic, fecal-commensal, and diarrheagenic Escherichia coli strains. tar and tsr were present or functional in nearly all isolates [16].
  • Low concentrations of L-[14C]serine specifically bound to wild-type membranes with a Km of 5 microM; in contrast, there was greatly decreased binding to vesicles prepared from the new mutants or from the tsr mutant AW518 [17].
  • The relationship between the chemoreceptor and thermoreceptor functions of Tsr was examined in five tsr mutants with altered serine detection thresholds [10].

Associations of tsr with chemical compounds

  • MCPI, the product of the tsr gene, accepts methyl groups at multiple sites that are located on two tryptic peptides, denoted K1 and R1 [13].
  • Typhimurium with mutations in the tsr (serine chemotaxis receptor protein) or oxrA (transcriptional regulator of anaerobic metabolism) genes did not inhibit colonisation [18].
  • Pleiotropic aspartate-taxis mutants (tar) showed normal thermoresponse but pleiotropic serine-taxis mutants (tsr) showed decreased or almost no thermoresponse [19].

Regulatory relationships of tsr

  • Thus, the presence of a cheX defect blocked the stimulus-elicited appearance of faster migrating forms of the tsr product; conversely, the presence of a cheB defect resulted in a pronounced shift toward these forms in the absence of a chemotactic stimulus [2].

Analytical, diagnostic and therapeutic context of tsr

  • Unlike tsr null mutants, cheD strains are generally nonchemotactic, dominant in complementation tests, and exhibit a pronounced counterclockwise bias in flagellar rotation [20].


  1. Structure of the serine chemoreceptor in Escherichia coli. Boyd, A., Kendall, K., Simon, M.I. Nature (1983) [Pubmed]
  2. Multiple electrophoretic forms of methyl-accepting chemotaxis proteins generated by stimulus-elicited methylation in Escherichia coli. Boyd, A., Simon, M.I. J. Bacteriol. (1980) [Pubmed]
  3. An Escherichia coli chemoreceptor gene is temporally controlled in Caulobacter. Frederikse, P.H., Shapiro, L. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  4. Gene disruption and gene replacement in Streptomyces via single stranded DNA transformation of integration vectors. Hillemann, D., Pühler, A., Wohlleben, W. Nucleic Acids Res. (1991) [Pubmed]
  5. Chemotactic methylation and behavior in Bacillus subtilis: role of two unique proteins, CheC and CheD. Rosario, M.M., Kirby, J.R., Bochar, D.A., Ordal, G.W. Biochemistry (1995) [Pubmed]
  6. Sensory transducers of E. coli are encoded by homologous genes. Boyd, A., Krikos, A., Simon, M. Cell (1981) [Pubmed]
  7. The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior. Rebbapragada, A., Johnson, M.S., Harding, G.P., Zuccarelli, A.J., Fletcher, H.M., Zhulin, I.B., Taylor, B.L. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  8. Novel sensory adaptation mechanism in bacterial chemotaxis to oxygen and phosphotransferase substrates. Niwano, M., Taylor, B.L. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  9. Nonheritable resistance to chloramphenicol and other antibiotics induced by salicylates and other chemotactic repellents in Escherichia coli K-12. Rosner, J.L. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  10. Thermosensing properties of Escherichia coli tsr mutants defective in serine chemoreception. Lee, L., Mizuno, T., Imae, Y. J. Bacteriol. (1988) [Pubmed]
  11. Multiple forms of methyl-accepting chemotaxis proteins distinguished by a factor in addition to multiple methylation. Hazelbauer, G.L., Engström, P. J. Bacteriol. (1981) [Pubmed]
  12. Evolution of chemotactic-signal transducers in enteric bacteria. Dahl, M.K., Boos, W., Manson, M.D. J. Bacteriol. (1989) [Pubmed]
  13. Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. Kehry, M.R., Bond, M.W., Hunkapiller, M.W., Dahlquist, F.W. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  14. Differentiation between electron transport sensing and proton motive force sensing by the Aer and Tsr receptors for aerotaxis. Edwards, J.C., Johnson, M.S., Taylor, B.L. Mol. Microbiol. (2006) [Pubmed]
  15. Identification of a site of ATP requirement for signal processing in bacterial chemotaxis. Smith, J.M., Rowsell, E.H., Shioi, J., Taylor, B.L. J. Bacteriol. (1988) [Pubmed]
  16. Uropathogenic Escherichia coli strains generally lack functional Trg and Tap chemoreceptors found in the majority of E. coli strains strictly residing in the gut. Lane, M.C., Lloyd, A.L., Markyvech, T.A., Hagan, E.C., Mobley, H.L. J. Bacteriol. (2006) [Pubmed]
  17. Genetic and biochemical properties of Escherichia coli mutants with defects in serine chemotaxis. Hedblom, M.L., Adler, J. J. Bacteriol. (1980) [Pubmed]
  18. Intestinal colonisation of gnotobiotic pigs by Salmonella organisms: interaction between isogenic and unrelated strains. Lovell, M.A., Barrow, P.A. J. Med. Microbiol. (1999) [Pubmed]
  19. Thermosensory transduction in Escherichia coli: inhibition of the thermoresponse by L-serine. Maeda, K., Imae, Y. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  20. Genetics of methyl-accepting chemotaxis proteins in Escherichia coli: cheD mutations affect the structure and function of the Tsr transducer. Callahan, A.M., Parkinson, J.S. J. Bacteriol. (1985) [Pubmed]
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