Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1995 Apr;177(7):1915–1917. doi: 10.1128/jb.177.7.1915-1917.1995

Molecular cloning of a 46-kilodalton surface antigen (P46) gene from Mycoplasma hyopneumoniae: direct evidence of CGG codon usage for arginine.

S Futo 1, Y Seto 1, S Mitsuse 1, Y Mori 1, T Suzuki 1, K Kawai 1
PMCID: PMC176830  PMID: 7896725

Abstract

The DNA sequence of the gene encoding the early and specific 46-kDa surface antigen (P46) of Mycoplasma hyopneumoniae has been determined. The P46 gene, encoding a putative lipoprotein, contained three TGA codons and a single CGG codon in a 1,257-bp open reading frame. Edman degradation of peptide fragments showed that at least one TGA codon encodes tryptophan and that the CGG codon, which has been reported to be nonsense or unassigned in other mycoplasmas, is used for arginine in M. hyopneumoniae.

Full Text

The Full Text of this article is available as a PDF (213.2 KB).

Selected References

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

  1. Haldimann A., Nicolet J., Frey J. DNA sequence determination and biochemical analysis of the immunogenic protein P36, the lactate dehydrogenase (LDH) of Mycoplasma hyopneumoniae. J Gen Microbiol. 1993 Feb;139(2):317–323. doi: 10.1099/00221287-139-2-317. [DOI] [PubMed] [Google Scholar]
  2. Hayashi S., Wu H. C. Lipoproteins in bacteria. J Bioenerg Biomembr. 1990 Jun;22(3):451–471. doi: 10.1007/BF00763177. [DOI] [PubMed] [Google Scholar]
  3. Inamine J. M., Ho K. C., Loechel S., Hu P. C. Evidence that UGA is read as a tryptophan codon rather than as a stop codon by Mycoplasma pneumoniae, Mycoplasma genitalium, and Mycoplasma gallisepticum. J Bacteriol. 1990 Jan;172(1):504–506. doi: 10.1128/jb.172.1.504-506.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Kim M. F., Heidari M. B., Stull S. J., McIntosh M. A., Wise K. S. Identification and mapping of an immunogenic region of Mycoplasma hyopneumoniae p65 surface lipoprotein expressed in Escherichia coli from a cloned genomic fragment. Infect Immun. 1990 Aug;58(8):2637–2643. doi: 10.1128/iai.58.8.2637-2643.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Mizushima S. Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli. Mol Cell Biochem. 1984;60(1):5–15. doi: 10.1007/BF00226297. [DOI] [PubMed] [Google Scholar]
  6. Mori Y., Hamaoka T., Sato S., Takeuchi S. Immunoblotting analysis of antibody response in swine experimentally inoculated with Mycoplasma hyopneumoniae. Vet Immunol Immunopathol. 1988 Oct;19(3-4):239–250. doi: 10.1016/0165-2427(88)90111-0. [DOI] [PubMed] [Google Scholar]
  7. Mori Y., Hamaoka T., Sato S. Use of monoclonal antibody in an enzyme-linked immunosorbent assay (ELISA) for the detection of antibodies against Mycoplasma hyopneumoniae. Isr J Med Sci. 1987 Jun;23(6):657–662. [PubMed] [Google Scholar]
  8. Nakamura K., Inouye M. DNA sequence of the gene for the outer membrane lipoprotein of E. coli: an extremely AT-rich promoter. Cell. 1979 Dec;18(4):1109–1117. doi: 10.1016/0092-8674(79)90224-1. [DOI] [PubMed] [Google Scholar]
  9. Neugebauer K., Sprengel R., Schaller H. Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium. Nucleic Acids Res. 1981 Jun 11;9(11):2577–2588. doi: 10.1093/nar/9.11.2577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Oba T., Andachi Y., Muto A., Osawa S. CGG: an unassigned or nonsense codon in Mycoplasma capricolum. Proc Natl Acad Sci U S A. 1991 Feb 1;88(3):921–925. doi: 10.1073/pnas.88.3.921. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Osawa S., Jukes T. H., Watanabe K., Muto A. Recent evidence for evolution of the genetic code. Microbiol Rev. 1992 Mar;56(1):229–264. doi: 10.1128/mr.56.1.229-264.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem. 1987 Nov 1;166(2):368–379. doi: 10.1016/0003-2697(87)90587-2. [DOI] [PubMed] [Google Scholar]
  14. Suzuki T., Ichihara S., Mizushima S. Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli. J Biochem. 1988 Mar;103(3):470–473. doi: 10.1093/oxfordjournals.jbchem.a122294. [DOI] [PubMed] [Google Scholar]
  15. Taschke C., Klinkert M. Q., Pirkl E., Herrmann R. Gene expression signals in Mycoplasma hyopneumoniae and Mycoplasma capricolum. Isr J Med Sci. 1987 May;23(5):347–351. [PubMed] [Google Scholar]
  16. Taschke C., Klinkert M. Q., Wolters J., Herrmann R. Organization of the ribosomal RNA genes in Mycoplasma hyopneumoniae: the 5S rRNA gene is separated from the 16S and 23S rRNA genes. Mol Gen Genet. 1986 Dec;205(3):428–433. doi: 10.1007/BF00338078. [DOI] [PubMed] [Google Scholar]
  17. Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 1987;153:3–11. doi: 10.1016/0076-6879(87)53044-0. [DOI] [PubMed] [Google Scholar]
  18. Weinberger C., Hollenberg S. M., Ong E. S., Harmon J. M., Brower S. T., Cidlowski J., Thompson E. B., Rosenfeld M. G., Evans R. M. Identification of human glucocorticoid receptor complementary DNA clones by epitope selection. Science. 1985 May 10;228(4700):740–742. doi: 10.1126/science.2581314. [DOI] [PubMed] [Google Scholar]
  19. Yamao F., Muto A., Kawauchi Y., Iwami M., Iwagami S., Azumi Y., Osawa S. UGA is read as tryptophan in Mycoplasma capricolum. Proc Natl Acad Sci U S A. 1985 Apr;82(8):2306–2309. doi: 10.1073/pnas.82.8.2306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Yogev D., Sela S., Bercovier H., Razin S. Nucleotide sequence and codon usage of the elongation factor Tu(EF-Tu) gene from Mycoplasma pneumoniae. Mol Microbiol. 1990 Aug;4(8):1303–1310. doi: 10.1111/j.1365-2958.1990.tb00709.x. [DOI] [PubMed] [Google Scholar]
  21. Young R. A., Davis R. W. Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194–1198. doi: 10.1073/pnas.80.5.1194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Yu F., Inouye S., Inouye M. Lipoprotein-28, a cytoplasmic membrane lipoprotein from Escherichia coli. Cloning, DNA sequence, and expression of its gene. J Biol Chem. 1986 Feb 15;261(5):2284–2288. [PubMed] [Google Scholar]

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

RESOURCES