Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1981 Jan;145(1):35–42. doi: 10.1128/jb.145.1.35-42.1981

Multiple forms of methyl-accepting chemotaxis proteins distinguished by a factor in addition to multiple methylation.

G L Hazelbauer, P Engström
PMCID: PMC217241  PMID: 7007319

Abstract

Methyl-accepting chemotaxis proteins are central to both the excitation and adaptation phases of chemotactic behavior. Using null mutations in the genes coding for the two major methyl-accepting proteins (tsr and tar), we identified the gene products among the membrane proteins of Escherichia coli visualized on one- and two-dimensional gels. On two-dimensional gels, both the tsr and the tar proteins appeared as a group of multiple spots arranged in two to four diagonal arrays. The multiplicity of forms could not be completely explained by the previously documented heterogeneity of the methylated proteins resulting from different numbers of methylated glutamyl residues per polypeptide chain. We suggest that there is at least one other way besides extent of methylation in which the polypeptides of a methylated protein can differ.

Full text

PDF

Images in this article

37Image
on p.37
38Image
on p.38
39Image
on p.39
40Image
on p.40
40Image
on p.40
41Image
on p.41

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adler J. Chemotaxis in bacteria. Science. 1966 Aug 12;153(3737):708–716. doi: 10.1126/science.153.3737.708. [DOI] [PubMed] [Google Scholar]
  2. Ames G. F., Nikaido K. Two-dimensional gel electrophoresis of membrane proteins. Biochemistry. 1976 Feb 10;15(3):616–623. doi: 10.1021/bi00648a026. [DOI] [PubMed] [Google Scholar]
  3. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  4. Boyd A., Simon M. I. Multiple electrophoretic forms of methyl-accepting chemotaxis proteins generated by stimulus-elicited methylation in Escherichia coli. J Bacteriol. 1980 Aug;143(2):809–815. doi: 10.1128/jb.143.2.809-815.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chelsky D., Dahlquist F. W. Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites. Proc Natl Acad Sci U S A. 1980 May;77(5):2434–2438. doi: 10.1073/pnas.77.5.2434. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. DeFranco A. L., Koshland D. E., Jr Multiple methylation in processing of sensory signals during bacterial chemotaxis. Proc Natl Acad Sci U S A. 1980 May;77(5):2429–2433. doi: 10.1073/pnas.77.5.2429. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DeFranco A. L., Parkinson J. S., Koshland D. E., Jr Functional homology of chemotaxis genes in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1979 Jul;139(1):107–114. doi: 10.1128/jb.139.1.107-114.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Engström P., Hazelbauer G. L. Multiple methylation of methyl-accepting chemotaxis proteins during adaptation of E. coli to chemical stimuli. Cell. 1980 May;20(1):165–171. doi: 10.1016/0092-8674(80)90244-5. [DOI] [PubMed] [Google Scholar]
  9. Goy M. F., Springer M. S., Adler J. Failure of sensory adaptation in bacterial mutants that are defective in a protein methylation reaction. Cell. 1978 Dec;15(4):1231–1240. doi: 10.1016/0092-8674(78)90049-1. [DOI] [PubMed] [Google Scholar]
  10. Harayama S., Palva E. T., Hazelbauer G. L. Transposon-insertion mutants of Escherichia coli K12 defective in a component common to galactose and ribose chemotaxis. Mol Gen Genet. 1979 Mar 20;171(2):193–203. doi: 10.1007/BF00270005. [DOI] [PubMed] [Google Scholar]
  11. Hayashi H., Koiwai O., Kozuka M. Studies on bacterial chemotaxis. II. Effect of cheB and cheZ mutations on the methylation of methyl-accepting chemotaxis protein of Escherichia coli. J Biochem. 1979 May;85(5):1213–1223. [PubMed] [Google Scholar]
  12. Hazelbauer G. L., Engström P. Parallel pathways for transduction of chemotactic signals in Escherichia coli. Nature. 1980 Jan 3;283(5742):98–100. doi: 10.1038/283098a0. [DOI] [PubMed] [Google Scholar]
  13. Hazelbauer G. L., Harayama S. Mutants in transmission of chemotactic signals from two independent receptors of E. coli. Cell. 1979 Mar;16(3):617–625. doi: 10.1016/0092-8674(79)90035-7. [DOI] [PubMed] [Google Scholar]
  14. Hazelbauer G. L., Mesibov R. E., Adler J. Escherichia coli mutants defective in chemotaxis toward specific chemicals. Proc Natl Acad Sci U S A. 1969 Dec;64(4):1300–1307. doi: 10.1073/pnas.64.4.1300. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kleene S. J., Toews M. L., Adler J. Isolation of glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis. J Biol Chem. 1977 May 25;252(10):3214–3218. [PubMed] [Google Scholar]
  16. Kondoh H., Ball C. B., Adler J. Identification of a methyl-accepting chemotaxis protein for the ribose and galactose chemoreceptors of Escherichia coli. Proc Natl Acad Sci U S A. 1979 Jan;76(1):260–264. doi: 10.1073/pnas.76.1.260. [DOI] [PMC free article] [PubMed] [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 U S A. 1975 Oct;72(10):3939–3943. doi: 10.1073/pnas.72.10.3939. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  19. Matsumura P., Silverman M., Simon M. Synthesis of mot and che gene products of Escherichia coli programmed by hybrid ColE1 plasmids in minicells. J Bacteriol. 1977 Dec;132(3):996–1002. doi: 10.1128/jb.132.3.996-1002.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  21. Parkinson J. S. Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis. J Bacteriol. 1978 Jul;135(1):45–53. doi: 10.1128/jb.135.1.45-53.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Randall L. L., Hardy S. J. Synthesis of exported proteins by membrane-bound polysomes from Escherichia coli. Eur J Biochem. 1977 May 2;75(1):43–53. doi: 10.1111/j.1432-1033.1977.tb11502.x. [DOI] [PubMed] [Google Scholar]
  23. Reader R. W., Tso W. W., Springer M. S., Goy M. F., Adler J. Pleiotropic aspartate taxis and serine taxis mutants of Escherichia coli. J Gen Microbiol. 1979 Apr;111(2):363–374. doi: 10.1099/00221287-111-2-363. [DOI] [PubMed] [Google Scholar]
  24. Ridgway H. G., Silverman M., Simon M. I. Localization of proteins controlling motility and chemotaxis in Escherichia coli. J Bacteriol. 1977 Nov;132(2):657–665. doi: 10.1128/jb.132.2.657-665.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Silerman M., Matsumura P., Draper R., Edwards S., Simon M. I. Expression of flagellar genes carried by bacteriophage lambda. Nature. 1976 May 20;261(5557):248–250. doi: 10.1038/261248a0. [DOI] [PubMed] [Google Scholar]
  26. Silverman M., Simon M. Chemotaxis in Escherichia coli: methylation of che gene products. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3317–3321. doi: 10.1073/pnas.74.8.3317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Springer M. S., Goy M. F., Adler J. Protein methylation in behavioural control mechanisms and in signal transduction. Nature. 1979 Jul 26;280(5720):279–284. doi: 10.1038/280279a0. [DOI] [PubMed] [Google Scholar]
  28. Springer M. S., Goy M. F., Adler J. Sensory transduction in Escherichia coli: two complementary pathways of information processing that involve methylated proteins. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3312–3316. doi: 10.1073/pnas.74.8.3312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Springer W. R., Koshland D. E., Jr Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system. Proc Natl Acad Sci U S A. 1977 Feb;74(2):533–537. doi: 10.1073/pnas.74.2.533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Stock J. B., Koshland D. E., Jr A protein methylesterase involved in bacterial sensing. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3659–3663. doi: 10.1073/pnas.75.8.3659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Van Der Werf P., Koshland D. E., Jr Identification of a gamma-glutamyl methyl ester in bacterial membrane protein involved in chemotaxis. J Biol Chem. 1977 Apr 25;252(8):2793–2795. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES