Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1991 Feb;173(4):1530–1535. doi: 10.1128/jb.173.4.1530-1535.1991

Complete nucleotide sequences and comparison of the structural genes of two 2-haloalkanoic acid dehalogenases from Pseudomonas sp. strain CBS3.

B Schneider 1, R Müller 1, R Frank 1, F Lingens 1
PMCID: PMC207292  PMID: 1995594

Abstract

The nucleotide sequences of two DNA segments from Pseudomonas sp. strain CBS3 that code for two different haloalkanoic acid halidohydrolases were determined. Two open reading frames with coding capacities of 227 amino acids (corresponding to a molecular mass of 25,401 Da) and 229 amino acids (corresponding to a molecular mass of 25,683 Da) were identified as structural genes of 2-haloalkanoic acid dehalogenases I (dehCI) and II (dehCII) by comparison with the N-terminal amino acid sequences of these enzymes. Comparison of the two sequences revealed 45% homology on the DNA level and 37.5% homology on the amino acid level. No homology with other known protein or nucleotide sequences was found.

Full text

PDF
1534

Images in this article

Selected References

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

  1. Clewell D. B., Helinski D. R. Supercoiled circular DNA-protein complex in Escherichia coli: purification and induced conversion to an opern circular DNA form. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1159–1166. doi: 10.1073/pnas.62.4.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  3. Ghosal D., You I. S., Chatterjee D. K., Chakrabarty A. M. Microbial degradation of halogenated compounds. Science. 1985 Apr 12;228(4696):135–142. doi: 10.1126/science.228.4696.135. [DOI] [PubMed] [Google Scholar]
  4. Goldman P., Milne G. W., Keister D. B. Carbon-halogen bond cleavage. 3. Studies on bacterial halidohrolases. J Biol Chem. 1968 Jan 25;243(2):428–434. [PubMed] [Google Scholar]
  5. Holmes D. S., Quigley M. A rapid boiling method for the preparation of bacterial plasmids. Anal Biochem. 1981 Jun;114(1):193–197. doi: 10.1016/0003-2697(81)90473-5. [DOI] [PubMed] [Google Scholar]
  6. Janssen D. B., Pries F., van der Ploeg J., Kazemier B., Terpstra P., Witholt B. Cloning of 1,2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10 and expression and sequencing of the dhlA gene. J Bacteriol. 1989 Dec;171(12):6791–6799. doi: 10.1128/jb.171.12.6791-6799.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Klages U., Krauss S., Lingens F. 2-Haloacid dehalogenase from a 4-chlorobenzoate-degrading Pseudomonas spec. CBS 3. Hoppe Seylers Z Physiol Chem. 1983 May;364(5):529–535. doi: 10.1515/bchm2.1983.364.1.529. [DOI] [PubMed] [Google Scholar]
  8. Klages U., Markus A., Lingens F. Degradation of 4-chlorophenylacetic acid by a Pseudomonas species. J Bacteriol. 1981 Apr;146(1):64–68. doi: 10.1128/jb.146.1.64-68.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kyhse-Andersen J. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods. 1984 Dec;10(3-4):203–209. doi: 10.1016/0165-022x(84)90040-x. [DOI] [PubMed] [Google Scholar]
  10. La Roche S. D., Leisinger T. Sequence analysis and expression of the bacterial dichloromethane dehalogenase structural gene, a member of the glutathione S-transferase supergene family. J Bacteriol. 1990 Jan;172(1):164–171. doi: 10.1128/jb.172.1.164-171.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mandel M., Higa A. Calcium-dependent bacteriophage DNA infection. J Mol Biol. 1970 Oct 14;53(1):159–162. doi: 10.1016/0022-2836(70)90051-3. [DOI] [PubMed] [Google Scholar]
  12. Motosugi K., Soda K. Microbial degradation of synthetic organochlorine compounds. Experientia. 1983 Nov 15;39(11):1214–1220. doi: 10.1007/BF01990358. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Slater J. H., Weightman A. J., Hall B. G. Dehalogenase genes of Pseudomonas putida PP3 on chromosomally located transposable elements. Mol Biol Evol. 1985 Nov;2(6):557–567. doi: 10.1093/oxfordjournals.molbev.a040366. [DOI] [PubMed] [Google Scholar]
  15. Smith J. M., Harrison K., Colby J. Purification and characterization of D-2-haloacid dehalogenase from Pseudomonas putida strain AJ1/23. J Gen Microbiol. 1990 May;136(5):881–886. doi: 10.1099/00221287-136-5-881. [DOI] [PubMed] [Google Scholar]
  16. Tautz D., Renz M. An optimized freeze-squeeze method for the recovery of DNA fragments from agarose gels. Anal Biochem. 1983 Jul 1;132(1):14–19. doi: 10.1016/0003-2697(83)90419-0. [DOI] [PubMed] [Google Scholar]
  17. Weightman A. J., Weightman A. L., Slater J. H. Stereospecificity of 2-monochloropropionate dehalogenation by the two dehalogenases of Pseudomonas putida PP3: evidence for two different dehalogenation mechanisms. J Gen Microbiol. 1982 Aug;128(8):1755–1762. doi: 10.1099/00221287-128-8-1755. [DOI] [PubMed] [Google Scholar]
  18. Wickramasinghe N. C. Galactic component of the diffuse X-ray background. Nature. 1970 Jul 18;227(5255):265–266. doi: 10.1038/227265a0. [DOI] [PubMed] [Google Scholar]
  19. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]

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

RESOURCES