Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1986 Jun;166(3):1007–1012. doi: 10.1128/jb.166.3.1007-1012.1986

Sequence of the flaA (cheC) locus of Escherichia coli and discovery of a new gene.

S C Kuo, D E Koshland Jr
PMCID: PMC215225  PMID: 3519573

Abstract

The flaA (cheC) locus from Escherichia coli is important in controlling the rotational direction of flagella during chemotaxis. The locus was sequenced, and a site of transcriptional initiation was determined. Two reading frames, flaAI and flaAII, span the locus. flaAII corresponds to certain flaA and cheC mutations, and has some unusual features in the predicted secondary structure. flaAI, however, has not been identified previously, but a flaAI deletion, which produced a truncated FlaAI peptide in minicells, clearly identified the FlaAI protein.

Full text

PDF
1012

Images in this article

1011Image
on p.1011
1011Image
on p.1011

Selected References

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

  1. Ames G. F. Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. J Biol Chem. 1974 Jan 25;249(2):634–644. [PubMed] [Google Scholar]
  2. Argos P., Hanei M., Garavito R. M. The Chou-Fasman secondary structure prediction method with an extended data base. FEBS Lett. 1978 Sep 1;93(1):19–24. doi: 10.1016/0014-5793(78)80795-9. [DOI] [PubMed] [Google Scholar]
  3. Armstrong J. B., Adler J. Complementation of nonchemotactic mutants of Escherichia coli. Genetics. 1969 Jan;61(1):61–66. doi: 10.1093/genetics/61.1.61. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Berg H. C., Brown D. A. Chemotaxis in Escherichia coli analysed by three-dimensional tracking. Nature. 1972 Oct 27;239(5374):500–504. doi: 10.1038/239500a0. [DOI] [PubMed] [Google Scholar]
  5. Biggin M. D., Gibson T. J., Hong G. F. Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination. Proc Natl Acad Sci U S A. 1983 Jul;80(13):3963–3965. doi: 10.1073/pnas.80.13.3963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chou P. Y., Fasman G. D. Structural and functional role of leucine residues in proteins. J Mol Biol. 1973 Mar 5;74(3):263–281. doi: 10.1016/0022-2836(73)90372-0. [DOI] [PubMed] [Google Scholar]
  7. Clegg D. O., Koshland D. E., Jr Identification of a bacterial sensing protein and effects of its elevated expression. J Bacteriol. 1985 Apr;162(1):398–405. doi: 10.1128/jb.162.1.398-405.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Davis R. W., Thomas M., Cameron J., St John T. P., Scherer S., Padgett R. A. Rapid DNA isolations for enzymatic and hybridization analysis. Methods Enzymol. 1980;65(1):404–411. doi: 10.1016/s0076-6879(80)65051-4. [DOI] [PubMed] [Google Scholar]
  9. Gilman M. Z., Chamberlin M. J. Developmental and genetic regulation of Bacillus subtilis genes transcribed by sigma 28-RNA polymerase. Cell. 1983 Nov;35(1):285–293. doi: 10.1016/0092-8674(83)90231-3. [DOI] [PubMed] [Google Scholar]
  10. Higgins C. F., Haag P. D., Nikaido K., Ardeshir F., Garcia G., Ames G. F. Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium. Nature. 1982 Aug 19;298(5876):723–727. doi: 10.1038/298723a0. [DOI] [PubMed] [Google Scholar]
  11. Kaiser E. T., Kézdy F. J. Amphiphilic secondary structure: design of peptide hormones. Science. 1984 Jan 20;223(4633):249–255. doi: 10.1126/science.6322295. [DOI] [PubMed] [Google Scholar]
  12. Khan S., Macnab R. M., DeFranco A. L., Koshland D. E., Jr Inversion of a behavioral response in bacterial chemotaxis: explanation at the molecular level. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4150–4154. doi: 10.1073/pnas.75.9.4150. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Komeda Y., Shimada K., Iino T. Isolation of specialized lambda transducing bacteriophages for flagellar genes (fla) of Escherichia coli K-12. J Virol. 1977 Jun;22(3):654–661. doi: 10.1128/jvi.22.3.654-661.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kondoh H. Tumbling chemotaxis mutants of Escherichia coli: possible gene-dependent effect of methionine starvation. J Bacteriol. 1980 May;142(2):527–534. doi: 10.1128/jb.142.2.527-534.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Macnab R. M., Aizawa S. Bacterial motility and the bacterial flagellar motor. Annu Rev Biophys Bioeng. 1984;13:51–83. doi: 10.1146/annurev.bb.13.060184.000411. [DOI] [PubMed] [Google Scholar]
  18. Macnab R. M., Koshland D. E., Jr The gradient-sensing mechanism in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2509–2512. doi: 10.1073/pnas.69.9.2509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  20. Meagher R. B., Tait R. C., Betlach M., Boyer H. W. Protein expression in E. coli minicells by recombinant plasmids. Cell. 1977 Mar;10(3):521–536. doi: 10.1016/0092-8674(77)90039-3. [DOI] [PubMed] [Google Scholar]
  21. Meselson M., Yuan R. DNA restriction enzyme from E. coli. Nature. 1968 Mar 23;217(5134):1110–1114. doi: 10.1038/2171110a0. [DOI] [PubMed] [Google Scholar]
  22. Messing J., Crea R., Seeburg P. H. A system for shotgun DNA sequencing. Nucleic Acids Res. 1981 Jan 24;9(2):309–321. doi: 10.1093/nar/9.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Parkinson J. S., Parker S. R. Interaction of the cheC and cheZ gene products is required for chemotactic behavior in Escherichia coli. Proc Natl Acad Sci U S A. 1979 May;76(5):2390–2394. doi: 10.1073/pnas.76.5.2390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. 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]
  26. Parkinson J. S. cheA, cheB, and cheC genes of Escherichia coli and their role in chemotaxis. J Bacteriol. 1976 May;126(2):758–770. doi: 10.1128/jb.126.2.758-770.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Ravid S., Eisenbach M. Direction of flagellar rotation in bacterial cell envelopes. J Bacteriol. 1984 Apr;158(1):222–230. doi: 10.1128/jb.158.1.222-230.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Rosenberg M., Court D. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet. 1979;13:319–353. doi: 10.1146/annurev.ge.13.120179.001535. [DOI] [PubMed] [Google Scholar]
  29. Rubik B. A., Koshland D. E., Jr Potentiation, desensitization, and inversion of response in bacterial sensing of chemical stimuli. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2820–2824. doi: 10.1073/pnas.75.6.2820. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Schiffer M., Edmundson A. B. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys J. 1967 Mar;7(2):121–135. doi: 10.1016/S0006-3495(67)86579-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Silverman M., Simon M. Genetic analysis of bacteriophage Mu-induced flagellar mutants in Escherichia coli. J Bacteriol. 1973 Oct;116(1):114–122. doi: 10.1128/jb.116.1.114-122.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Silverman M., Simon M. Genetic analysis of flagellar mutants in Escherichia coli. J Bacteriol. 1973 Jan;113(1):105–113. doi: 10.1128/jb.113.1.105-113.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Warrick H. M., Taylor B. L., Koshland D. E., Jr Chemotactic mechanism of Salmonella typhimurium: preliminary mapping and characterization of mutants. J Bacteriol. 1977 Apr;130(1):223–231. doi: 10.1128/jb.130.1.223-231.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Yamaguchi S., Fujita H., Ishihara A., Aizawa S., Macnab R. M. Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching. J Bacteriol. 1986 Apr;166(1):187–193. doi: 10.1128/jb.166.1.187-193.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES