Abstract
The CO dehydrogenase structural genes (cox) and orf4 are clustered in the transcriptional order coxM--> coxS--> coxL--> orf4 on the 128-kb megaplasmid pHCG3 of the carboxidotroph Oligotropha carboxidovorans OM5. Sequence analysis suggested association of molybdopterin cytosine dinucleotide and flavin adenine dinucleotide with CoxL and of the [2Fe-2S] clusters with CoxS.
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- Amaya Y., Yamazaki K., Sato M., Noda K., Nishino T., Nishino T. Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin. J Biol Chem. 1990 Aug 25;265(24):14170–14175. [PubMed] [Google Scholar]
- Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bray R. C., George G. N., Lange R., Meyer O. Studies by e.p.r. spectroscopy of carbon monoxide oxidases from Pseudomonas carboxydovorans and Pseudomonas carboxydohydrogena. Biochem J. 1983 Jun 1;211(3):687–694. doi: 10.1042/bj2110687. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Davidson B. E., Sajgò M., Noller H. F., Harris J. I. Amino-acid sequence of glyceraldehyde 3-phosphate dehydrogenase from lobster muscle. Nature. 1967 Dec 23;216(5121):1181–1185. doi: 10.1038/2161181a0. [DOI] [PubMed] [Google Scholar]
- Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
- Grether-Beck S., Igloi G. L., Pust S., Schilz E., Decker K., Brandsch R. Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol Microbiol. 1994 Sep;13(5):929–936. doi: 10.1111/j.1365-2958.1994.tb00484.x. [DOI] [PubMed] [Google Scholar]
- Harayama S., Polissi A., Rekik M. Divergent evolution of chloroplast-type ferredoxins. FEBS Lett. 1991 Jul 8;285(1):85–88. doi: 10.1016/0014-5793(91)80730-q. [DOI] [PubMed] [Google Scholar]
- 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]
- Houde M., Tiveron M. C., Brégégère F. Divergence of the nucleotide sequences encoding xanthine dehydrogenase in Calliphora vicina and Drosophila melanogaster. Gene. 1989 Dec 28;85(2):391–402. doi: 10.1016/0378-1119(89)90432-0. [DOI] [PubMed] [Google Scholar]
- Hugendieck I., Meyer O. The structural genes encoding CO dehydrogenase subunits (cox L, M and S) in Pseudomonas carboxydovorans OM5 reside on plasmid pHCG3 and are, with the exception of Streptomyces thermoautotrophicus, conserved in carboxydotrophic bacteria. Arch Microbiol. 1992;157(3):301–304. doi: 10.1007/BF00245166. [DOI] [PubMed] [Google Scholar]
- Hughes R. K., Doyle W. A., Chovnick A., Whittle J. R., Burke J. F., Bray R. C. Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase. Biochem J. 1992 Jul 15;285(Pt 2):507–513. doi: 10.1042/bj2850507. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hughes R. K. Xanthine dehydrogenase from Drosophila melanogaster: purification and properties of the wild-type enzyme and of a variant lacking iron-sulfur centers. Biochemistry. 1992 Mar 31;31(12):3073–3083. doi: 10.1021/bi00127a007. [DOI] [PubMed] [Google Scholar]
- Johnson J. L., Rajagopalan K. V., Meyer O. Isolation and characterization of a second molybdopterin dinucleotide: molybdopterin cytosine dinucleotide. Arch Biochem Biophys. 1990 Dec;283(2):542–545. doi: 10.1016/0003-9861(90)90681-n. [DOI] [PubMed] [Google Scholar]
- Karplus P. A., Daniels M. J., Herriott J. R. Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. Science. 1991 Jan 4;251(4989):60–66. [PubMed] [Google Scholar]
- Keith T. P., Riley M. A., Kreitman M., Lewontin R. C., Curtis D., Chambers G. Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster. Genetics. 1987 May;116(1):67–73. doi: 10.1093/genetics/116.1.67. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kita K., Oya H., Gennis R. B., Ackrell B. A., Kasahara M. Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur (Ip) subunit of liver mitochondria. Biochem Biophys Res Commun. 1990 Jan 15;166(1):101–108. doi: 10.1016/0006-291x(90)91916-g. [DOI] [PubMed] [Google Scholar]
- Kraut M., Hugendieck I., Herwig S., Meyer O. Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria. Arch Microbiol. 1989;152(4):335–341. doi: 10.1007/BF00425170. [DOI] [PubMed] [Google Scholar]
- Krauth-Siegel R. L., Blatterspiel R., Saleh M., Schiltz E., Schirmer R. H., Untucht-Grau R. Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259–267. doi: 10.1111/j.1432-1033.1982.tb05780.x. [DOI] [PubMed] [Google Scholar]
- 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]
- Lee C. S., Curtis D., McCarron M., Love C., Gray M., Bender W., Chovnick A. Mutations affecting expression of the rosy locus in Drosophila melanogaster. Genetics. 1987 May;116(1):55–66. doi: 10.1093/genetics/116.1.55. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meyer O. Chemical and spectral properties of carbon monoxide: methylene blue oxidoreductase. The molybdenum-containing iron-sulfur flavoprotein from Pseudomonas carboxydovorans. J Biol Chem. 1982 Feb 10;257(3):1333–1341. [PubMed] [Google Scholar]
- Möller W., Amons R. Phosphate-binding sequences in nucleotide-binding proteins. FEBS Lett. 1985 Jul 1;186(1):1–7. doi: 10.1016/0014-5793(85)81326-0. [DOI] [PubMed] [Google Scholar]
- Riley M. A. Nucleotide sequence of the Xdh region in Drosophila pseudoobscura and an analysis of the evolution of synonymous codons. Mol Biol Evol. 1989 Jan;6(1):33–52. doi: 10.1093/oxfordjournals.molbev.a040529. [DOI] [PubMed] [Google Scholar]
- Russel M., Model P. Replacement of the fip gene of Escherichia coli by an inactive gene cloned on a plasmid. J Bacteriol. 1984 Sep;159(3):1034–1039. doi: 10.1128/jb.159.3.1034-1039.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rypniewski W. R., Breiter D. R., Benning M. M., Wesenberg G., Oh B. H., Markley J. L., Rayment I., Holden H. M. Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry. 1991 Apr 30;30(17):4126–4131. doi: 10.1021/bi00231a003. [DOI] [PubMed] [Google Scholar]
- Tabor S., Richardson C. C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc Natl Acad Sci U S A. 1985 Feb;82(4):1074–1078. doi: 10.1073/pnas.82.4.1074. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Terao M., Cazzaniga G., Ghezzi P., Bianchi M., Falciani F., Perani P., Garattini E. Molecular cloning of a cDNA coding for mouse liver xanthine dehydrogenase. Regulation of its transcript by interferons in vivo. Biochem J. 1992 May 1;283(Pt 3):863–870. doi: 10.1042/bj2830863. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thoenes U., Flores O. L., Neves A., Devreese B., Van Beeumen J. J., Huber R., Romão M. J., LeGall J., Moura J. J., Rodrigues-Pousada C. Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxido-reductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase. Eur J Biochem. 1994 Mar 15;220(3):901–910. doi: 10.1111/j.1432-1033.1994.tb18693.x. [DOI] [PubMed] [Google Scholar]
- Tsukihira T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H. X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 A resolution. J Biochem. 1981 Dec;90(6):1763–1773. doi: 10.1093/oxfordjournals.jbchem.a133654. [DOI] [PubMed] [Google Scholar]
- Von Zabern I., Wittmann-Liebold B., Untucht-Grau R., Schirmer R. H., Pai E. F. Primary and tertiary structure of the principal human adenylate kinase. Eur J Biochem. 1976 Sep;68(1):281–290. doi: 10.1111/j.1432-1033.1976.tb10787.x. [DOI] [PubMed] [Google Scholar]
- Weijer W. J., Hofsteenge J., Beintema J. J., Wierenga R. K., Drenth J. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure. Eur J Biochem. 1983 Jun 1;133(1):109–118. doi: 10.1111/j.1432-1033.1983.tb07435.x. [DOI] [PubMed] [Google Scholar]
- Wootton J. C., Nicolson R. E., Cock J. M., Walters D. E., Burke J. F., Doyle W. A., Bray R. C. Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim Biophys Acta. 1991 Mar 29;1057(2):157–185. doi: 10.1016/s0005-2728(05)80100-8. [DOI] [PubMed] [Google Scholar]