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Volumn 16, Issue 3, 2005, Pages 207-216

Characterisation of the 11 Kb DNA region adjacent to the gene encoding Desulfovibrio gigas flavoredoxin

Author keywords

Desulfovibrio gigas; Flanking regions; Flavoredoxin; Monocystronic

Indexed keywords

BINDING PROTEIN; COENZYME A; FLAVOREDOXIN; LIPOPROTEIN; MESSENGER RNA; RIBOSOME RNA; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 24044519688     PISSN: 10425179     EISSN: 10292365     Source Type: Journal    
DOI: 10.1080/10425170500088296     Document Type: Article
Times cited : (2)

References (41)
  • 3
    • 0030923669 scopus 로고    scopus 로고
    • Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction
    • Aoki H, Adams SL, Turner MA, Ganoza MC. 1997. Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction. Biochimie 79:7-11.
    • (1997) Biochimie , vol.79 , pp. 7-11
    • Aoki, H.1    Adams, S.L.2    Turner, M.A.3    Ganoza, M.C.4
  • 4
    • 0033302071 scopus 로고    scopus 로고
    • An evolutionary classification of the metallo-beta-lactamase fold proteins
    • Aravind L. 1999. An evolutionary classification of the metallo-beta-lactamase fold proteins. In Silico Biol 1:69-91.
    • (1999) In Silico Biol , vol.1 , pp. 69-91
    • Aravind, L.1
  • 5
    • 0033046425 scopus 로고    scopus 로고
    • Novel predicted RNA-binding domains associated with the translation machinery
    • Aravind L, Koonin EV. 1999. Novel predicted RNA-binding domains associated with the translation machinery. J Mol Evol 48:291-302.
    • (1999) J Mol Evol , vol.48 , pp. 291-302
    • Aravind, L.1    Koonin, E.V.2
  • 8
    • 0014968396 scopus 로고
    • JV6-(Delta 2-isopentenyl)adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli
    • Bartz JK, Kline LK, Söll D. 1970. JV6-(Delta 2-isopentenyl) adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli. Biochem Biophys Res Commun 40:1481-1487.
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 1481-1487
    • Bartz, J.K.1    Kline, L.K.2    Söll, D.3
  • 9
    • 0028839886 scopus 로고
    • A new Escherichia coli cell division gene,fts K
    • Begg KJ, Dewar SJ, Donachie WD. 1995. A new Escherichia coli cell division gene,fts K. J Bacteriol 177:6211-6222.
    • (1995) J Bacteriol , vol.177 , pp. 6211-6222
    • Begg, K.J.1    Dewar, S.J.2    Donachie, W.D.3
  • 11
  • 12
    • 0022412657 scopus 로고
    • E. coli ribosomal protein operons: The case of the misplaced genes
    • Bjork GR. 1985. E. coli ribosomal protein operons: The case of the misplaced genes. Cell 42:7-8.
    • (1985) Cell , vol.42 , pp. 7-8
    • Bjork, G.R.1
  • 13
    • 0033929248 scopus 로고    scopus 로고
    • All major regions of FtsK are required for resolution of chromosome dimers
    • Boyle DS, Grant D, Draper GC, Donachie WD. 2000. All major regions of FtsK are required for resolution of chromosome dimers. J Bacteriol 182:4124-4127.
    • (2000) J Bacteriol , vol.182 , pp. 4124-4127
    • Boyle, D.S.1    Grant, D.2    Draper, G.C.3    Donachie, W.D.4
  • 14
    • 0037102538 scopus 로고    scopus 로고
    • Metallo-beta-lactamase fold within nucleic acids processing enzymes: The beta-CASP family
    • Callebaut I, Moshous D, Mornon JP, de Villartay JP. 2002. Metallo-beta-lactamase fold within nucleic acids processing enzymes: The beta-CASP family. Nucleic Acids Res 30: 3592-3601.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3592-3601
    • Callebaut, I.1    Moshous, D.2    Mornon, J.P.3    De Villartay, J.P.4
  • 15
    • 0027179553 scopus 로고
    • Isolation and characterization of flavoredoxin, a new flavoprotein that permits in vitro reconstitution of an electron transfer chain from molecular hydrogen to sulfite reduction in the bacterium Desulfovibrio gigas
    • Chen L, Liu MY, LeGall J. 1993. Isolation and characterization of flavoredoxin, a new flavoprotein that permits in vitro reconstitution of an electron transfer chain from molecular hydrogen to sulfite reduction in the bacterium Desulfovibrio gigas. Arch Biochem Biophys 303:44-50.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 44-50
    • Chen, L.1    Liu, M.Y.2    Legall, J.3
  • 16
    • 0024371122 scopus 로고
    • Genetic and physiological relationships among the miaA. gene, 2-methylthio-N6-(delta 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12
    • Connolly DM, Winkler ME. 1989. Genetic and physiological relationships among the miaA. gene, 2-methylthio-N6-(delta 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12. J Bacteriol 171:3233-3246.
    • (1989) J Bacteriol , vol.171 , pp. 3233-3246
    • Connolly, D.M.1    Winkler, M.E.2
  • 17
    • 0033053644 scopus 로고    scopus 로고
    • 16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli: Deletion, mutation of the conserved Asp 102 residue, and sequence comparison among all other pseudouridine synthases
    • Conrad J, Niu L, Rudd K, Lane BG, Ofengand J. 1999. 16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli: Deletion, mutation of the conserved Asp 102 residue, and sequence comparison among all other pseudouridine synthases. RNA 5:751-763.
    • (1999) RNA , vol.5 , pp. 751-763
    • Conrad, J.1    Niu, L.2    Rudd, K.3    Lane, B.G.4    Ofengand, J.5
  • 18
    • 0034725994 scopus 로고    scopus 로고
    • Membrane topology of the N-terminus of the Escherichia coli FtsK division protein
    • Dorazi R, Dewar SJ. 2000. Membrane topology of the N-terminus of the Escherichia coli FtsK division protein. FEBS Lett 478: 13-18.
    • (2000) FEBS Lett , vol.478 , pp. 13-18
    • Dorazi, R.1    Dewar, S.J.2
  • 19
    • 1842376275 scopus 로고    scopus 로고
    • The modified nucleoside 2-methylthio-N6-isopentenyladenosine in tRNA of Shigella flexneri is required for expression of virulence genes
    • Durand JM, Bjork GR, Kuwae A, Yoshikawa M, Sasakawa C. 1997. The modified nucleoside 2-methylthio-N6-isopentenyladenosine in tRNA of Shigella flexneri is required for expression of virulence genes. J Bacteriol 179:5777-5782.
    • (1997) J Bacteriol , vol.179 , pp. 5777-5782
    • Durand, J.M.1    Bjork, G.R.2    Kuwae, A.3    Yoshikawa, M.4    Sasakawa, C.5
  • 20
    • 0033965439 scopus 로고    scopus 로고
    • Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: The expression of the vir F gene
    • Durand JM, Dagberg B, Uhlin BE, Bjork GR. 2000. Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: The expression of the vir F gene. Mol Microbiol 35:924-935.
    • (2000) Mol Microbiol , vol.35 , pp. 924-935
    • Durand, J.M.1    Dagberg, B.2    Uhlin, B.E.3    Bjork, G.R.4
  • 22
    • 0033578920 scopus 로고    scopus 로고
    • Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli
    • Geerlof A, Lewendon A, Shaw WV. 1999. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J Biol Chem 274:27105-27111.
    • (1999) J Biol Chem , vol.274 , pp. 27105-27111
    • Geerlof, A.1    Lewendon, A.2    Shaw, W.V.3
  • 23
    • 0030954667 scopus 로고    scopus 로고
    • Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin
    • Gomes CM, Suva G, Oliveira S, LeGall J, Liu MY, Xavier AV, Rodrigues-Pousada C, Teixeira M. 1997. Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin. J Biol Chem 272:22502-22508.
    • (1997) J Biol Chem , vol.272 , pp. 22502-22508
    • Gomes, C.M.1    Suva, G.2    Oliveira, S.3    Legall, J.4    Liu, M.Y.5    Xavier, A.V.6    Rodrigues-Pousada, C.7    Teixeira, M.8
  • 24
    • 0026531622 scopus 로고
    • Mutation of the miaA gene of Agrobacterium tumefaciens results in reduced vir gene expression
    • Gray J, Wang J, Gelvin SB. 1992. Mutation of the miaA gene of Agrobacterium tumefaciens results in reduced vir gene expression. J Bacteriol 174:1086-1098.
    • (1992) J Bacteriol , vol.174 , pp. 1086-1098
    • Gray, J.1    Wang, J.2    Gelvin, S.B.3
  • 26
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann K, Stoffel W 1993. TMbase-A database of membrane spanning proteins segments. Biol Chem Hoppe-Seyler 374:166.
    • (1993) Biol Chem Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 27
    • 0033561042 scopus 로고    scopus 로고
    • The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity
    • Izard T, Geerlof A. 1999. The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity. EMBO J 18:2021-2030.
    • (1999) EMBO J , vol.18 , pp. 2021-2030
    • Izard, T.1    Geerlof, A.2
  • 28
    • 0024744277 scopus 로고
    • Cloning and sequencing of the nifH gene of Desulfovibrio gigas
    • Kent HM, Buck M, Evans DJ. 1989. Cloning and sequencing of the nifH gene of Desulfovibrio gigas. FEMS Microbiol Lett 61:73-78.
    • (1989) FEMS Microbiol Lett , vol.61 , pp. 73-78
    • Kent, H.M.1    Buck, M.2    Evans, D.J.3
  • 29
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar S, Tamura K, Jakobsen IB, Nei M. 2001. MEGA2: Molecular evolutionary genetics analysis software. Bioinformatics 17:1244-1245.
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 30
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. 1982. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 31
    • 0031039226 scopus 로고    scopus 로고
    • Physiological characteristics and growth behavior of single and double hydrogenase mutants of Desulfovibrio fructosovorans
    • Malki S, De Luca G, Fardeau ML, Rousset M, Belaich JP, Dermoun Z. 1997. Physiological characteristics and growth behavior of single and double hydrogenase mutants of Desulfovibrio fructosovorans. Arch Microbiol 167:38-45.
    • (1997) Arch Microbiol , vol.167 , pp. 38-45
    • Malki, S.1    De Luca, G.2    Fardeau, M.L.3    Rousset, M.4    Belaich, J.P.5    Dermoun, Z.6
  • 32
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone T, Blumenthal RM, Cheng X. 1995. Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes. J Mol Biol 253:618-632.
    • (1995) J Mol Biol , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 34
    • 0344588103 scopus 로고
    • Physiological diversity of sulfate-reducing bacteria
    • Tuovinen EOH, editor. Colombus: Ohio State University Press
    • Peck HD. 1984. Physiological diversity of sulfate-reducing bacteria. In: Tuovinen EOH, editor. Microbial chemoautothrophy. Colombus: Ohio State University Press, p 309-335.
    • (1984) Microbial Chemoautothrophy , pp. 309-335
    • Peck, H.D.1
  • 37
    • 0023375195 scopus 로고
    • The neighbor-joining methods: Anew method for constructing phylogenetic trees
    • Saitou M, Nei M. 1987. The neighbor-joining methods: Anew method for constructing phylogenetic trees. Mol Biol Evol 4:406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, M.1    Nei, M.2
  • 39
    • 0034666108 scopus 로고    scopus 로고
    • STRING: A web-server to retrieve and display the repeatedly occurring neighbourhood of a gene
    • Snel B, Lehmann G, Bork P, Huynen MA. 2000. STRING: A web-server to retrieve and display the repeatedly occurring neighbourhood of a gene. Nucleic Acids Res 28:3442-3444.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3442-3444
    • Snel, B.1    Lehmann, G.2    Bork, P.3    Huynen, M.A.4
  • 40
    • 0034668039 scopus 로고    scopus 로고
    • DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases
    • Szegedi SS, Gumport RI. 2000. DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases. Nucleic Acids Res 28:3972-3981.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3972-3981
    • Szegedi, S.S.1    Gumport, R.I.2
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.