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. 1995 Jan;61(1):290–296. doi: 10.1128/aem.61.1.290-296.1995

Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR.

R R Karkhoff-Schweizer 1, D P Huber 1, G Voordouw 1
PMCID: PMC167283  PMID: 7887608

Abstract

The structural genes for dissimilatory sulfite reductase (desulfoviridin) from Desulfovibrio vulgaris Hilden-borough were cloned as a 7.2-kbp SacII DNA fragment. Nucleotide sequencing indicated the presence of a third gene, encoding a protein of only 78 amino acids, immediately downstream from the genes for the alpha and beta subunits (dsvA and dsvB). We designated this protein DsvD and the gene encoding it the dsvD gene. The alpha- and beta-subunit sequences are highly homologous to those of the dissimilatory sulfite reductase from Archaeoglobus fulgidus, a thermophilic archaeal sulfate reducer, which grows optimally at 83 degrees C. A gene with significant homology to dsvD was also found immediately downstream from the dsrAB genes of A. fulgidus. The remarkable conservation of gene arrangement and sequence across domain (bacterial versus archaeal) and physical (mesophilic versus thermophilic) boundaries indicates an essential role for DsvD in dissimilatory sulfite reduction and allowed the construction of conserved deoxyoligonucleotide primers for detection of the dissimilatory sulfite reductase genes in the environment.

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Selected References

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  1. Brumlik M. J., Voordouw G. Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris Hildenborough. J Bacteriol. 1989 Sep;171(9):4996–5004. doi: 10.1128/jb.171.9.4996-5004.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dahl C., Kredich N. M., Deutzmann R., Trüper H. G. Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes. J Gen Microbiol. 1993 Aug;139(8):1817–1828. doi: 10.1099/00221287-139-8-1817. [DOI] [PubMed] [Google Scholar]
  3. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ebina Y., Nakazawa A. Cyclic AMP-dependent initiation and rho-dependent termination of colicin E1 gene transcription. J Biol Chem. 1983 Jun 10;258(11):7072–7078. [PubMed] [Google Scholar]
  5. Karkhoff-Schweizer R. R., Bruschi M., Voordouw G. Expression of the gamma-subunit gene of desulfoviridin-type dissimilatory sulfite reductase and of the alpha- and beta-subunit genes is not coordinately regulated. Eur J Biochem. 1993 Feb 1;211(3):501–507. doi: 10.1111/j.1432-1033.1993.tb17576.x. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Lee J. P., LeGall J., Peck H. D., Jr Isolation of assimilatroy- and dissimilatory-type sulfite reductases from Desulfovibrio vulgaris. J Bacteriol. 1973 Aug;115(2):529–542. doi: 10.1128/jb.115.2.529-542.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Pierik A. J., Duyvis M. G., van Helvoort J. M., Wolbert R. B., Hagen W. R. The third subunit of desulfoviridin-type dissimilatory sulfite reductases. Eur J Biochem. 1992 Apr 1;205(1):111–115. doi: 10.1111/j.1432-1033.1992.tb16757.x. [DOI] [PubMed] [Google Scholar]
  9. Pollock W. B., Chemerika P. J., Forrest M. E., Beatty J. T., Voordouw G. Expression of the gene encoding cytochrome c3 from Desulfovibrio vulgaris (Hildenborough) in Escherichia coli: export and processing of the apoprotein. J Gen Microbiol. 1989 Aug;135(8):2319–2328. doi: 10.1099/00221287-135-8-2319. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Staden R. Graphic methods to determine the function of nucleic acid sequences. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 2):521–538. doi: 10.1093/nar/12.1part2.521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Staden R., McLachlan A. D. Codon preference and its use in identifying protein coding regions in long DNA sequences. Nucleic Acids Res. 1982 Jan 11;10(1):141–156. doi: 10.1093/nar/10.1.141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Tan J., Helms L. R., Swenson R. P., Cowan J. A. Primary structure of the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough): cloning and nucleotide sequence of the reductase gene. Biochemistry. 1991 Oct 15;30(41):9900–9907. doi: 10.1021/bi00105a013. [DOI] [PubMed] [Google Scholar]
  14. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Voordouw G., Shen Y., Harrington C. S., Telang A. J., Jack T. R., Westlake D. W. Quantitative reverse sample genome probing of microbial communities and its application to oil field production waters. Appl Environ Microbiol. 1993 Dec;59(12):4101–4114. doi: 10.1128/aem.59.12.4101-4114.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Voordouw G., Voordouw J. K., Jack T. R., Foght J., Fedorak P. M., Westlake D. W. Identification of distinct communities of sulfate-reducing bacteria in oil fields by reverse sample genome probing. Appl Environ Microbiol. 1992 Nov;58(11):3542–3552. doi: 10.1128/aem.58.11.3542-3552.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Voordouw G., Voordouw J. K., Karkhoff-Schweizer R. R., Fedorak P. M., Westlake D. W. Reverse sample genome probing, a new technique for identification of bacteria in environmental samples by DNA hybridization, and its application to the identification of sulfate-reducing bacteria in oil field samples. Appl Environ Microbiol. 1991 Nov;57(11):3070–3078. doi: 10.1128/aem.57.11.3070-3078.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. 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]

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