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Volumn 145, Issue 6, 1999, Pages 1421-1429

Characterization of a molybdenum cofactor biosynthetic gene cluster in Rhodobacter capsulatus which is specific for the biogenesis of dimethylsulfoxide reductase

Author keywords

Dimethylsulfoxide reductase; Molybdenum cofactor; Rhodobacter capsulatus

Indexed keywords

BACTERIAL ENZYME; DIMETHYL SULFOXIDE REDUCTASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 0033056056     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-145-6-1421     Document Type: Article
Times cited : (19)

References (53)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R. H. & Munck, E. (1997). Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 111, 653-659.
    • (1997) Science , vol.111 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 2
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. C. (1996). A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22, 393-404.
    • (1996) Mol Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 4
    • 0021770582 scopus 로고
    • A computer algorithm for testing potential prokaryotic terminators
    • Brendel, V. & Trifonov, E. N. (1984). A computer algorithm for testing potential prokaryotic terminators. Nucleic Acids Res 12, 4411-4427.
    • (1984) Nucleic Acids Res , vol.12 , pp. 4411-4427
    • Brendel, V.1    Trifonov, E.N.2
  • 5
    • 0022409586 scopus 로고
    • Determination of the metabolic origin of the sulfur atom in thiamine of Escherichia coli by mass spectrometry
    • DeMoll, E. & Shive, W. (1985). Determination of the metabolic origin of the sulfur atom in thiamine of Escherichia coli by mass spectrometry. Biochem Biophys Res Commun 132, 217-222.
    • (1985) Biochem Biophys Res Commun , vol.132 , pp. 217-222
    • DeMoll, E.1    Shive, W.2
  • 6
    • 0027967844 scopus 로고
    • How proteins cross the bacterial cytoplasmic membrane
    • Driessen, A. J. M. (1994). How proteins cross the bacterial cytoplasmic membrane. J Membr Biol 142, 145-159.
    • (1994) J Membr Biol , vol.142 , pp. 145-159
    • Driessen, A.J.M.1
  • 7
    • 0028858745 scopus 로고
    • Identification and isolation of a gene required for nitrate assimilation and anaerobic growth of Bacillus subtilis
    • Glaser, P., Danchin, A., Kunst, F., Zuber, P. & Nakano, M. M. (1995). Identification and isolation of a gene required for nitrate assimilation and anaerobic growth of Bacillus subtilis. J Bacteriol 177, 1112-1115.
    • (1995) J Bacteriol , vol.177 , pp. 1112-1115
    • Glaser, P.1    Danchin, A.2    Kunst, F.3    Zuber, P.4    Nakano, M.M.5
  • 8
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdoenzymes
    • Hille, R. (1996). The mononuclear molybdoenzymes. Chem Rev 96, 2757-2816.
    • (1996) Chem Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 9
    • 0021286821 scopus 로고
    • A physical map of pPH1J1 and pJB4JI
    • Hirsch, P. R. & Beringer, J. E. (1984). A physical map of pPH1J1 and pJB4JI. Plasmid 12, 139-141.
    • (1984) Plasmid , vol.12 , pp. 139-141
    • Hirsch, P.R.1    Beringer, J.E.2
  • 10
    • 0023120320 scopus 로고
    • In vitro synthesis of molybdopterin
    • Johnson, J. L. & Rajagopalan, K. V. (1987a). In vitro synthesis of molybdopterin. J Bacteriol 169, 110-116.
    • (1987) J Bacteriol , vol.169 , pp. 110-116
    • Johnson, J.L.1    Rajagopalan, K.V.2
  • 11
    • 0023135158 scopus 로고
    • Involvement of chlA, chlE, chlM and chlN loci in Escherichia coli molybdopterin biosynthesis
    • Johnson, J. L. & Rajagopalan, K. V. (1987b). Involvement of chlA, chlE, chlM and chlN loci in Escherichia coli molybdopterin biosynthesis. J Bacteriol 169, 117-125.
    • (1987) J Bacteriol , vol.169 , pp. 117-125
    • Johnson, J.L.1    Rajagopalan, K.V.2
  • 12
    • 0021723025 scopus 로고
    • Transposon Tn5 mutagenesis of genes for the photosynthetic apparatus in Rhodopseudomonas capsulata
    • Kaufmann, N., Hudig, H. & Drews, G. (1984). Transposon Tn5 mutagenesis of genes for the photosynthetic apparatus in Rhodopseudomonas capsulata. Mol Gen Genet 198, 153-158.
    • (1984) Mol Gen Genet , vol.198 , pp. 153-158
    • Kaufmann, N.1    Hudig, H.2    Drews, G.3
  • 13
    • 0019087876 scopus 로고
    • Iron-sulfur proteins: Spin coupling models for three-iron clusters
    • Kent, T. A., Huynh, B. H. & Munck, E. (1980). Iron-sulfur proteins: spin coupling models for three-iron clusters. Proc Natl Acad Sci USA 77, 6574-6576.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6574-6576
    • Kent, T.A.1    Huynh, B.H.2    Munck, E.3
  • 14
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum cofactor-containing enzymes: Structure and mechanism
    • Kisker, C., Schindelin, H. & Rees, D. C. (1997). Molybdenum cofactor-containing enzymes: structure and mechanism. Annu Rev Biochem 66, 233-267.
    • (1997) Annu Rev Biochem , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0031940235 scopus 로고    scopus 로고
    • Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdoenzymes
    • Leimkuhler, S., Kern, P. S., Solomon, P. S., McEwan, A. G., Schwarz, G., Mendel, R. R. & Klipp, W. (1998). Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdoenzymes. Mol Microbiol 27, 853-869.
    • (1998) Mol Microbiol , vol.27 , pp. 853-869
    • Leimkuhler, S.1    Kern, P.S.2    Solomon, P.S.3    McEwan, A.G.4    Schwarz, G.5    Mendel, R.R.6    Klipp, W.7
  • 18
    • 0031444936 scopus 로고    scopus 로고
    • Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: Crystal structure of the oxidised enzyme at 1·82 Å resolution and the dithionite-reduced enzyme at 2-8 Å resolution
    • McAlpine, A. S., McEwan, A. G., Shaw, A. L. & Bailey, S. (1997). Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1·82 Å resolution and the dithionite-reduced enzyme at 2-8 Å resolution. J Biol Inorg Chem 2, 690-701.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 690-701
    • McAlpine, A.S.1    McEwan, A.G.2    Shaw, A.L.3    Bailey, S.4
  • 19
    • 0021331749 scopus 로고
    • Rationalisation of the properties of nitrate reductases from Rhodopseudomonas capsulata
    • McEwan, A. G., Jackson, J. B. & Ferguson, S. J. (1984). Rationalisation of the properties of nitrate reductases from Rhodopseudomonas capsulata. Arch Microbiol 137, 344-349.
    • (1984) Arch Microbiol , vol.137 , pp. 344-349
    • McEwan, A.G.1    Jackson, J.B.2    Ferguson, S.J.3
  • 20
    • 0021913760 scopus 로고
    • Periplasmic location of the terminal oxidoreductase in trimethylamine-N-oxide and dimethylsulphoxide respiration in the photosynthetic bacterium Rhodopseudomonas capsulata
    • McEwan, A. G., Wetzstein, H. G., Ferguson, S. J. & Jackson, J. B. (1985). Periplasmic location of the terminal oxidoreductase in trimethylamine-N-oxide and dimethylsulphoxide respiration in the photosynthetic bacterium Rhodopseudomonas capsulata. Biochim Biophys Acta 806, 410-417.
    • (1985) Biochim Biophys Acta , vol.806 , pp. 410-417
    • McEwan, A.G.1    Wetzstein, H.G.2    Ferguson, S.J.3    Jackson, J.B.4
  • 21
    • 0026065682 scopus 로고
    • Purification and properties of dimethylsulphoxide reductase from Rhodobacter capsulatus
    • McEwan, A. G., Ferguson, S. J. & Jackson, J. B. (1991). Purification and properties of dimethylsulphoxide reductase from Rhodobacter capsulatus. Biochem J 207, 305-307.
    • (1991) Biochem J , vol.207 , pp. 305-307
    • McEwan, A.G.1    Ferguson, S.J.2    Jackson, J.B.3
  • 22
    • 0023952240 scopus 로고
    • Genetic characterisation and sequence analysis of the duplicated nifA/nifB gene region of Rhodobacter capsulatus
    • Masepohl, B., Klipp, W. & Puhler, A. (1988). Genetic characterisation and sequence analysis of the duplicated nifA/nifB gene region of Rhodobacter capsulatus. Mol Gen Genet 212, 27-37.
    • (1988) Mol Gen Genet , vol.212 , pp. 27-37
    • Masepohl, B.1    Klipp, W.2    Puhler, A.3
  • 23
    • 0028982741 scopus 로고
    • A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: Characterisation and site-directed mutagenesis of the encoded protein
    • Menendez, C., Igloi, G., Henninger, H. & Brandsch, R. (1995). A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterisation and site-directed mutagenesis of the encoded protein. Arch Microbiot 164, 142-151.
    • (1995) Arch Microbiot , vol.164 , pp. 142-151
    • Menendez, C.1    Igloi, G.2    Henninger, H.3    Brandsch, R.4
  • 24
    • 0242500553 scopus 로고    scopus 로고
    • MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo-pterin cofactor biosynthesis is an Fe-S protein
    • Menendez, C., Sibert, D. & Brandsch, R. (1996). MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo-pterin cofactor biosynthesis is an Fe-S protein. FEBS Lett 391, 101-103.
    • (1996) FEBS Lett , vol.391 , pp. 101-103
    • Menendez, C.1    Sibert, D.2    Brandsch, R.3
  • 25
    • 0027421636 scopus 로고
    • Electron paramagnetic resonance
    • Pilbrow, J. R. & Hanson, G. R. (1993). Electron paramagnetic resonance. Methods Enzymol 227, 330-353.
    • (1993) Methods Enzymol , vol.227 , pp. 330-353
    • Pilbrow, J.R.1    Hanson, G.R.2
  • 26
    • 0024352039 scopus 로고
    • Two proteins encoded at the chlA locus constitute the converting factor of Escherichia coli chlA1
    • Pitterle, D. M. & Rajagopalan, K. V. (1989). Two proteins encoded at the chlA locus constitute the converting factor of Escherichia coli chlA1. J Bacteriol 171, 3373-3378.
    • (1989) J Bacteriol , vol.171 , pp. 3373-3378
    • Pitterle, D.M.1    Rajagopalan, K.V.2
  • 27
    • 0027490597 scopus 로고
    • The biosynthesis of molybdopterin. Purification and characterization of the converting factor
    • Pitterle, D. M., Johnson, J. L. & Rajagopalan, K. V. (1993). The biosynthesis of molybdopterin. Purification and characterization of the converting factor. J Biol Chem 268, 13506-13509.
    • (1993) J Biol Chem , vol.268 , pp. 13506-13509
    • Pitterle, D.M.1    Johnson, J.L.2    Rajagopalan, K.V.3
  • 28
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley, A. G. (1993). The complete general secretory pathway in Gram-negative bacteria. Microbiol Rev 57, 10-108.
    • (1993) Microbiol Rev , vol.57 , pp. 10-108
    • Pugsley, A.G.1
  • 29
    • 0029881191 scopus 로고    scopus 로고
    • Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: Structural and functional differences among prokaryotic nitrate reductases
    • Reyes, F., Roldan, M. D., Klipp, W., Castillo, F. & Moreno-Vivian, C. (1996). Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases. Mol Microbiol 19, 1307-1318.
    • (1996) Mol Microbiol , vol.19 , pp. 1307-1318
    • Reyes, F.1    Roldan, M.D.2    Klipp, W.3    Castillo, F.4    Moreno-Vivian, C.5
  • 30
    • 0027298448 scopus 로고
    • Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis
    • Rivers, S. L., McNairn, E., Blasco, F., Giordano, G. & Boxer, D. H. (1993). Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Mol Microbiol 8, 1071-1081.
    • (1993) Mol Microbiol , vol.8 , pp. 1071-1081
    • Rivers, S.L.1    McNairn, E.2    Blasco, F.3    Giordano, G.4    Boxer, D.H.5
  • 32
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic translocation pathway in Escherichia coli
    • Santini, C.-L., Ize, B., Chanal, A., Muller, M., Giordano, G. & Wu, L.-F. (1998). A novel Sec-independent periplasmic translocation pathway in Escherichia coli. EMBO J 17, 101-112.
    • (1998) EMBO J , vol.17 , pp. 101-112
    • Santini, C.-L.1    Ize, B.2    Chanal, A.3    Muller, M.4    Giordano, G.5    Wu, L.-F.6
  • 33
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., Bogsch, E. G., Stanley, N. R., Wexler, M., Robinson, C., Berks, B. C. & Palmer, T. (1998). Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J 17, 3640-3650.
    • (1998) EMBO J , vol.17 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 34
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase : Redox-linked changes in molybdopterin coordination
    • Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K. V. & Rees, D. C. (1996). Crystal structure of DMSO reductase : Redox-linked changes in molybdopterin coordination. Science 272, 1615-1620.
    • (1996) Science , vol.272 , pp. 1615-1620
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 35
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of dimethylsulfoxide reductase from Rhodobacter capsulatus at 1-88 Å resolution
    • Schneider, F., Lowe, J., Huber, R., Schindelin, H., Kisker, C. & Knablein, J. (1996). Crystal structure of dimethylsulfoxide reductase from Rhodobacter capsulatus at 1-88 Å resolution. J Mol Biol 263, 53-69.
    • (1996) J Mol Biol , vol.263 , pp. 53-69
    • Schneider, F.1    Lowe, J.2    Huber, R.3    Schindelin, H.4    Kisker, C.5    Knablein, J.6
  • 37
    • 0000655643 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus
    • Shaw, A. L., Hanson, G. R. & McEwan, A. G. (1996). Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus. Biochim Biophys Acta 1276, 176-180.
    • (1996) Biochim Biophys Acta , vol.1276 , pp. 176-180
    • Shaw, A.L.1    Hanson, G.R.2    McEwan, A.G.3
  • 38
    • 0033049616 scopus 로고    scopus 로고
    • Mutational analysis of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter capsulatus
    • Shaw, A. L., Leimkuhler, S., Klipp, W., Hanson, G. R. & McEwan, A. G. (1999). Mutational analysis of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter capsulatus. Microbiology 145, 1409-1420.
    • (1999) Microbiology , vol.145 , pp. 1409-1420
    • Shaw, A.L.1    Leimkuhler, S.2    Klipp, W.3    Hanson, G.R.4    McEwan, A.G.5
  • 39
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., Priefer, U. & Puhler, A. (1983). A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1, 784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 44
    • 0027450492 scopus 로고
    • Structural genes for thiamine biosynthetic enzymes (thiCEFGH)
    • Vander Horn, P. B., Backstrom, A., Stewart, V. & Begley, T. P. (1993). Structural genes for thiamine biosynthetic enzymes (thiCEFGH). J Bacteriol 175, 982-992.
    • (1993) J Bacteriol , vol.175 , pp. 982-992
    • Vander Horn, P.B.1    Backstrom, A.2    Stewart, V.3    Begley, T.P.4
  • 45
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira, J. & Messing, J. (1982). The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19, 259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 46
    • 34047176349 scopus 로고
    • A new method for simulating randomly oriented powder spectra in magnetic resonance: The Sydney Opera House (SOPHE) method
    • Wang, D. & Hanson, G. R. (1995). A new method for simulating randomly oriented powder spectra in magnetic resonance: The Sydney Opera House (SOPHE) method. J Magn Reson A 111, 1-8.
    • (1995) J Magn Reson A , vol.111 , pp. 1-8
    • Wang, D.1    Hanson, G.R.2
  • 47
    • 0030352253 scopus 로고    scopus 로고
    • New methodologies for computer simulations of paramagnetic resonance spectra
    • Wang, D. & Hanson, G. R. (1996). New methodologies for computer simulations of paramagnetic resonance spectra. Appl Magn Reson 11, 401-415.
    • (1996) Appl Magn Reson , vol.11 , pp. 401-415
    • Wang, D.1    Hanson, G.R.2
  • 48
    • 0016720598 scopus 로고
    • Characterisation of Rhodopseudomonas capsulata
    • Weaver, P. F., Wall, J. D. & Gest, H. (1975). Characterisation of Rhodopseudomonas capsulata. Arch Microbiol 105, 207-216.
    • (1975) Arch Microbiol , vol.105 , pp. 207-216
    • Weaver, P.F.1    Wall, J.D.2    Gest, H.3
  • 49
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • Weiner, J. H., Bilous, P. T., Shaw, G. M., Lubitz, S. P., Frost, L., Thomas, G. H., Cole, J. H. & Turner, R. J. (1998). A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93, 93-101.
    • (1998) Cell , vol.93 , pp. 93-101
    • Weiner, J.H.1    Bilous, P.T.2    Shaw, G.M.3    Lubitz, S.P.4    Frost, L.5    Thomas, G.H.6    Cole, J.H.7    Turner, R.J.8
  • 50
    • 0026773516 scopus 로고
    • Identification of formate dehydrogenase-specific mRNA species and nucleotide sequence of the fdhC gene of Methanobacterium formicicum
    • White, W. B. & Ferry, J. G. (1992). Identification of formate dehydrogenase-specific mRNA species and nucleotide sequence of the fdhC gene of Methanobacterium formicicum. J Bacteriol 174, 4997-5004.
    • (1992) J Bacteriol , vol.174 , pp. 4997-5004
    • White, W.B.1    Ferry, J.G.2
  • 51
    • 0028819468 scopus 로고
    • Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labelling studies
    • Wuebbens, M. M. & Rajagopalan, K. V. (1995). Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labelling studies. J Biol Chem 270, 1082-1087.
    • (1995) J Biol Chem , vol.270 , pp. 1082-1087
    • Wuebbens, M.M.1    Rajagopalan, K.V.2
  • 52
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 53
    • 0025848026 scopus 로고
    • Molybdenum requirement for translocation of diemethylsulfoxide reductase to the periplasmic space in a photodenitrifier Rhodobacter sphaeroides f. sp. denitrificans
    • Yoshida, Y., Takai, M., Satoh, T. & Takami, S. (1991). Molybdenum requirement for translocation of diemethylsulfoxide reductase to the periplasmic space in a photodenitrifier Rhodobacter sphaeroides f. sp. denitrificans. J Bacteriol 173, 3277-3281.
    • (1991) J Bacteriol , vol.173 , pp. 3277-3281
    • Yoshida, Y.1    Takai, M.2    Satoh, T.3    Takami, S.4


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