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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1988 Sep;85(18):6711–6715. doi: 10.1073/pnas.85.18.6711

Acetyladenylate plays a role in controlling the direction of flagellar rotation.

A J Wolfe 1, M P Conley 1, H C Berg 1
PMCID: PMC282047  PMID: 2901103

Abstract

Cells of Escherichia coli deleted for genes that code for the transducers and all the known cytoplasmic Che proteins except CheY responded reversibly to the addition of acetate by spinning their flagellar motors clockwise. By varying growth conditions and using metabolic inhibitors and mutants deficient in acetate metabolism, this effect was shown to require acetate-CoA synthetase [acetate:CoA ligase (AMP-forming); EC 6.2.1.1], an enzyme that catalyzes the formation of acetyl-CoA from acetate by an acetyladenylate intermediate. A mutant deficient in this enzyme but retaining the chemotaxis genes was deficient for chemotaxis. Thus, acetyladenylate appears to play a role in generating clockwise rotation at the level of CheY or the motor.

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Selected References

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  1. Adler J. A method for measuring chemotaxis and use of the method to determine optimum conditions for chemotaxis by Escherichia coli. J Gen Microbiol. 1973 Jan;74(1):77–91. doi: 10.1099/00221287-74-1-77. [DOI] [PubMed] [Google Scholar]
  2. BERG P. Acyl adenylates; an enzymatic mechanism of acetate activation. J Biol Chem. 1956 Oct;222(2):991–1013. [PubMed] [Google Scholar]
  3. BROWN G. M. The metabolism of pantothenic acid. J Biol Chem. 1959 Feb;234(2):370–378. [PubMed] [Google Scholar]
  4. Brown T. D., Jones-Mortimer M. C., Kornberg H. L. The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. J Gen Microbiol. 1977 Oct;102(2):327–336. doi: 10.1099/00221287-102-2-327. [DOI] [PubMed] [Google Scholar]
  5. Clegg D. O., Koshland D. E., Jr The role of a signaling protein in bacterial sensing: behavioral effects of increased gene expression. Proc Natl Acad Sci U S A. 1984 Aug;81(16):5056–5060. doi: 10.1073/pnas.81.16.5056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cronan J. E., Jr, Littel K. J., Jackowski S. Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1982 Mar;149(3):916–922. doi: 10.1128/jb.149.3.916-922.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hedblom M. L., Adler J. Chemotactic response of Escherichia coli to chemically synthesized amino acids. J Bacteriol. 1983 Sep;155(3):1463–1466. doi: 10.1128/jb.155.3.1463-1466.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hess J. F., Oosawa K., Kaplan N., Simon M. I. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell. 1988 Apr 8;53(1):79–87. doi: 10.1016/0092-8674(88)90489-8. [DOI] [PubMed] [Google Scholar]
  9. Hess J. F., Oosawa K., Matsumura P., Simon M. I. Protein phosphorylation is involved in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7609–7613. doi: 10.1073/pnas.84.21.7609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jackowski S., Rock C. O. Regulation of coenzyme A biosynthesis. J Bacteriol. 1981 Dec;148(3):926–932. doi: 10.1128/jb.148.3.926-932.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kihara M., Macnab R. M. Cytoplasmic pH mediates pH taxis and weak-acid repellent taxis of bacteria. J Bacteriol. 1981 Mar;145(3):1209–1221. doi: 10.1128/jb.145.3.1209-1221.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kuo S. C., Koshland D. E., Jr Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coli. J Bacteriol. 1987 Mar;169(3):1307–1314. doi: 10.1128/jb.169.3.1307-1314.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Maloy S. R., Bohlander M., Nunn W. D. Elevated levels of glyoxylate shunt enzymes in Escherichia coli strains constitutive for fatty acid degradation. J Bacteriol. 1980 Aug;143(2):720–725. doi: 10.1128/jb.143.2.720-725.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ninfa A. J., Magasanik B. Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli. Proc Natl Acad Sci U S A. 1986 Aug;83(16):5909–5913. doi: 10.1073/pnas.83.16.5909. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Oosawa K., Hess J. F., Simon M. I. Mutants defective in bacterial chemotaxis show modified protein phosphorylation. Cell. 1988 Apr 8;53(1):89–96. doi: 10.1016/0092-8674(88)90490-4. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Parkinson J. S., Parker S. R., Talbert P. B., Houts S. E. Interactions between chemotaxis genes and flagellar genes in Escherichia coli. J Bacteriol. 1983 Jul;155(1):265–274. doi: 10.1128/jb.155.1.265-274.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. ROSE I. A., GRUNBERG-MANAGO M., KOREY S. R., OCHOA S. Enzymatic phosphorylation of acetate. J Biol Chem. 1954 Dec;211(2):737–756. [PubMed] [Google Scholar]
  19. Ravid S., Matsumura P., Eisenbach M. Restoration of flagellar clockwise rotation in bacterial envelopes by insertion of the chemotaxis protein CheY. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7157–7161. doi: 10.1073/pnas.83.19.7157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Repaske D. R., Adler J. Change in intracellular pH of Escherichia coli mediates the chemotactic response to certain attractants and repellents. J Bacteriol. 1981 Mar;145(3):1196–1208. doi: 10.1128/jb.145.3.1196-1208.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Ronson C. W., Nixon B. T., Ausubel F. M. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell. 1987 Jun 5;49(5):579–581. doi: 10.1016/0092-8674(87)90530-7. [DOI] [PubMed] [Google Scholar]
  22. Segall J. E., Ishihara A., Berg H. C. Chemotactic signaling in filamentous cells of Escherichia coli. J Bacteriol. 1985 Jan;161(1):51–59. doi: 10.1128/jb.161.1.51-59.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Senior P. J. Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J Bacteriol. 1975 Aug;123(2):407–418. doi: 10.1128/jb.123.2.407-418.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Shioi J. I., Galloway R. J., Niwano M., Chinnock R. E., Taylor B. L. Requirement of ATP in bacterial chemotaxis. J Biol Chem. 1982 Jul 25;257(14):7969–7975. [PubMed] [Google Scholar]
  25. Slonczewski J. L., Macnab R. M., Alger J. R., Castle A. M. Effects of pH and repellent tactic stimuli on protein methylation levels in Escherichia coli. J Bacteriol. 1982 Oct;152(1):384–399. doi: 10.1128/jb.152.1.384-399.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Stock A., Chen T., Welsh D., Stock J. CheA protein, a central regulator of bacterial chemotaxis, belongs to a family of proteins that control gene expression in response to changing environmental conditions. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1403–1407. doi: 10.1073/pnas.85.5.1403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Tso W. W., Adler J. Negative chemotaxis in Escherichia coli. J Bacteriol. 1974 May;118(2):560–576. doi: 10.1128/jb.118.2.560-576.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wolfe A. J., Conley M. P., Kramer T. J., Berg H. C. Reconstitution of signaling in bacterial chemotaxis. J Bacteriol. 1987 May;169(5):1878–1885. doi: 10.1128/jb.169.5.1878-1885.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Wylie D., Stock A., Wong C. Y., Stock J. Sensory transduction in bacterial chemotaxis involves phosphotransfer between Che proteins. Biochem Biophys Res Commun. 1988 Mar 15;151(2):891–896. doi: 10.1016/s0006-291x(88)80365-6. [DOI] [PubMed] [Google Scholar]
  30. Yamaguchi S., Aizawa S., Kihara M., Isomura M., Jones C. J., Macnab R. M. Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium. J Bacteriol. 1986 Dec;168(3):1172–1179. doi: 10.1128/jb.168.3.1172-1179.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]

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