Skip to main content
PMC home page
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
. 1989 Jan;86(2):424–428. doi: 10.1073/pnas.86.2.424

"Frizzy" aggregation genes of the gliding bacterium Myxococcus xanthus show sequence similarities to the chemotaxis genes of enteric bacteria.

M J McBride 1, R A Weinberg 1, D R Zusman 1
PMCID: PMC286482  PMID: 2492105

Abstract

The frz genes of Myxococcus xanthus are necessary for proper aggregation of cells to form fruiting bodies. Mutations in the frz genes affect the frequency with which individual cells reverse their direction of movement. We have subcloned and determined the nucleotide sequence of three of the frz genes. From the sequence we predict three open reading frames corresponding to frzA, frzB, and frzCD. The putative FrzA protein (17,094 Da) exhibits 28.1% amino acid identity with the CheW protein of Salmonella typhimurium. The putative FrzCD protein (43,571 Da) contains a region of about 250 amino acids which is similar to the C-terminal portions of the methyl-accepting chemotaxis receptor proteins of the enteric bacteria. FrzCD also contains a region with potentially significant similarity to the DNA-binding region of the Bacillus subtilis sigma 43. The putative FrzB protein (12,066 Da) shares no significant identity with known chemotaxis proteins. The sequence similarities between the putative Frz proteins and the chemotaxis proteins of the enteric bacteria strongly support the hypothesis that the frz genes define a system of signal transduction analogous to the enterobacterial chemotaxis systems.

Full text

PDF
425

Selected References

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

  1. Bibb M. J., Findlay P. R., Johnson M. W. The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences. Gene. 1984 Oct;30(1-3):157–166. doi: 10.1016/0378-1119(84)90116-1. [DOI] [PubMed] [Google Scholar]
  2. Blackhart B. D., Zusman D. R. "Frizzy" genes of Myxococcus xanthus are involved in control of frequency of reversal of gliding motility. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8767–8770. doi: 10.1073/pnas.82.24.8767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blackhart B. D., Zusman D. R. Analysis of the products of the Myxococcus xanthus frz genes. J Bacteriol. 1986 May;166(2):673–678. doi: 10.1128/jb.166.2.673-678.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blackhart B. D., Zusman D. R. Cloning and complementation analysis of the "Frizzy" genes of Myxococcus xanthus. Mol Gen Genet. 1985;198(2):243–254. doi: 10.1007/BF00383002. [DOI] [PubMed] [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 U S A. 1984 Jun;81(11):3287–3291. doi: 10.1073/pnas.81.11.3287. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chou P. Y., Fasman G. D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol. 1978;47:45–148. doi: 10.1002/9780470122921.ch2. [DOI] [PubMed] [Google Scholar]
  7. Dworkin M., Eide D. Myxococcus xanthus does not respond chemotactically to moderate concentration gradients. J Bacteriol. 1983 Apr;154(1):437–442. doi: 10.1128/jb.154.1.437-442.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gitt M. A., Wang L. F., Doi R. H. A strong sequence homology exists between the major RNA polymerase sigma factors of Bacillus subtilis and Escherichia coli. J Biol Chem. 1985 Jun 25;260(12):7178–7185. [PubMed] [Google Scholar]
  9. Hawley D. K., McClure W. R. Compilation and analysis of Escherichia coli promoter DNA sequences. Nucleic Acids Res. 1983 Apr 25;11(8):2237–2255. doi: 10.1093/nar/11.8.2237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Helmann J. D., Chamberlin M. J. DNA sequence analysis suggests that expression of flagellar and chemotaxis genes in Escherichia coli and Salmonella typhimurium is controlled by an alternative sigma factor. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6422–6424. doi: 10.1073/pnas.84.18.6422. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Henikoff S. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene. 1984 Jun;28(3):351–359. doi: 10.1016/0378-1119(84)90153-7. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Hunt T. P., Magasanik B. Transcription of glnA by purified Escherichia coli components: core RNA polymerase and the products of glnF, glnG, and glnL. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8453–8457. doi: 10.1073/pnas.82.24.8453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Krikos A., Conley M. P., Boyd A., Berg H. C., Simon M. I. Chimeric chemosensory transducers of Escherichia coli. Proc Natl Acad Sci U S A. 1985 Mar;82(5):1326–1330. doi: 10.1073/pnas.82.5.1326. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Krikos A., Mutoh N., Boyd A., Simon M. I. Sensory transducers of E. coli are composed of discrete structural and functional domains. Cell. 1983 Jun;33(2):615–622. doi: 10.1016/0092-8674(83)90442-7. [DOI] [PubMed] [Google Scholar]
  16. Oosawa K., Mutoh N., Simon M. I. Cloning of the C-terminal cytoplasmic fragment of the tar protein and effects of the fragment on chemotaxis of Escherichia coli. J Bacteriol. 1988 Jun;170(6):2521–2526. doi: 10.1128/jb.170.6.2521-2526.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ordal G. W. Bacterial chemotaxis: biochemistry of behavior in a single cell. Crit Rev Microbiol. 1985;12(2):95–130. doi: 10.3109/10408418509104426. [DOI] [PubMed] [Google Scholar]
  18. Parkinson J. S. Protein phosphorylation in bacterial chemotaxis. Cell. 1988 Apr 8;53(1):1–2. doi: 10.1016/0092-8674(88)90478-3. [DOI] [PubMed] [Google Scholar]
  19. Russo A. F., Koshland D. E., Jr Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing. Science. 1983 Jun 3;220(4601):1016–1020. doi: 10.1126/science.6302843. [DOI] [PubMed] [Google Scholar]
  20. Stock A., Mottonen J., Chen T., Stock J. Identification of a possible nucleotide binding site in CheW, a protein required for sensory transduction in bacterial chemotaxis. J Biol Chem. 1987 Jan 15;262(2):535–537. [PubMed] [Google Scholar]
  21. Terwilliger T. C., Wang J. Y., Koshland D. E., Jr Surface structure recognized for covalent modification of the aspartate receptor in chemotaxis. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6707–6710. doi: 10.1073/pnas.83.18.6707. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Zusman D. R. "Frizzy" mutants: a new class of aggregation-defective developmental mutants of Myxococcus xanthus. J Bacteriol. 1982 Jun;150(3):1430–1437. doi: 10.1128/jb.150.3.1430-1437.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES