메뉴 건너뛰기




Volumn 378, Issue 3-4, 1997, Pages 303-308

Organization of the DMSO Respiratory Operon of Rhodobactercapsulatus and Its Consequences for Homologous Expression of DMSOR/TMAOR

Author keywords

Cloning; Dimethyl sulfoxide reductase; Homologous expression; Respiratory operon; Rhodobacter capsulatus; Trimethylamine N oxide reductase

Indexed keywords

BACTERIAL ENZYME; OXIDOREDUCTASE;

EID: 0345070011     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.3-4.303     Document Type: Article
Times cited : (2)

References (31)
  • 2
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli
    • Bilous, P.T., Cole. S.T., Anderson, W.F., and Weiner, J.H. (1988). Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. Mol. Microbiol. 2.785-795.
    • (1988) Mol. Microbiol. , vol.2 , pp. 785-795
    • Bilous, P.T.1    Cole, S.T.2    Anderson, W.F.3    Weiner, J.H.4
  • 3
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA E. coli strain with beta-galactosidase selection
    • Bullock, W.O., Fernandez. J.M., and Short. J.M. (1987). XL1-Blue: A high efficiency plasmid transforming recA E. coli strain with beta-galactosidase selection. Bio Techniques, 376.
    • (1987) Bio Techniques , pp. 376
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 4
    • 0020793569 scopus 로고
    • A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A.R., and Vogelstein, B. (1983). A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 732.6-13.
    • (1983) Anal. Biochem. , vol.732 , pp. 6-13
    • Feinberg, A.R.1    Vogelstein, B.2
  • 5
    • 0021381028 scopus 로고
    • A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A.R., and Vogelstein. B. (1984). A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity. Addendum. Anal. Biochem. 137, 266-267.
    • (1984) Addendum. Anal. Biochem. , vol.137 , pp. 266-267
    • Feinberg, A.R.1    Vogelstein, B.2
  • 6
    • 0027407377 scopus 로고
    • Chromosomal structure of Rhodobacter capsulatus strain SB1003: cosmid encyclopedia and high-resolution physical and genetic map
    • Fonstein. M., and Haselkorn, R. (1993). Chromosomal structure of Rhodobacter capsulatus strain SB1003: cosmid encyclopedia and high-resolution physical and genetic map. Proc. Nat. Acad. Sci. USA 90, 2522-2526.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 2522-2526
    • Fonstein, M.1    Haselkorn, R.2
  • 7
    • 0026776436 scopus 로고
    • Physical map of the genome of Rhodobacter capsulatus SB 1003
    • Fonstein, M., Zheng, S., and Haselkorn, R. (1992). Physical map of the genome of Rhodobacter capsulatus SB 1003. J. Bacteriol. 774, 4070-4077.
    • (1992) J. Bacteriol. , vol.774 , pp. 4070-4077
    • Fonstein, M.1    Zheng, S.2    Haselkorn, R.3
  • 8
    • 0029067295 scopus 로고
    • Refinement of the high-resolution physical and genetic map of Rhodobacter capsulatus and genome surveys using blots of the cosmid encyclopedia
    • Fonstein, M., Koshy. E.G. Nikolskaya. T., Mourachov, P., and Haselkorn, R. (1995). Refinement of the high-resolution physical and genetic map of Rhodobacter capsulatus and genome surveys using blots of the cosmid encyclopedia. EMBO Journal 74, 1827-1841.
    • (1995) EMBO Journal , vol.74 , pp. 1827-1841
    • Fonstein, M.1    Koshy, E.G.2    Nikolskaya, T.3    Mourachov, P.4    Haselkorn, R.5
  • 9
    • 0029926237 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of Dimethyl Sulfoxide Reductase from Rhodobacter sphaeroides
    • George, G.N., Hilton, J., and Rajagopalan, K.V. (1996). X-ray absorption spectroscopy of Dimethyl Sulfoxide Reductase from Rhodobacter sphaeroides. J. Am. Chem. Soc. 178, 1113-1117.
    • (1996) J. Am. Chem. Soc. , vol.178 , pp. 1113-1117
    • George, G.N.1    Hilton, J.2    Rajagopalan, K.V.3
  • 11
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with Plasmids
    • Hanahan, D. (1983). Studies on transformation of Escherichia coli with Plasmids. J. Mol. Biol. 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 12
    • 0030592480 scopus 로고    scopus 로고
    • Isolation, cloning, sequence analysis and localization of the operon encoding Dimethyl Sulfoxide/Trimethylamine N-oxide Reductase from Rhodobacter capsulatus
    • Knablein. J. Mann, K., Ehlert, S. Fonstein, M., Huber, R., and Schneider, F (1996). Isolation, cloning, sequence analysis and localization of the operon encoding Dimethyl Sulfoxide/Trimethylamine N-oxide Reductase from Rhodobacter capsulatus. J. Mol. Boi. 263, 40-52
    • (1996) J. Mol. Boi. , vol.263 , pp. 40-52
    • Knablein, J.1    Mann, K.2    Ehlert, S.3    Fonstein, M.4    Huber, R.5    Schneider, F.6
  • 13
    • 0023134480 scopus 로고
    • Amino-terminal amino acid sequences of electron transfer proteins from Gram-negative bacteria as indicators of their cellular localization: the sulphate reducing bacteria
    • LeGall, J., and Peck, H.D. (1987). Amino-terminal amino acid sequences of electron transfer proteins from Gram-negative bacteria as indicators of their cellular localization: the sulphate reducing bacteria. FEMS Microbiol Rev 46.35-40.
    • (1987) FEMS Microbiol Rev , vol.46 , pp. 35-40
    • LeGall, J.1    Peck, H.D.2
  • 14
    • 0028556393 scopus 로고
    • Photosynthetic electron transport and anaerobic metabolism in purple non-sulfur phototrophic bacteria
    • McEwan. A.G. (1994). Photosynthetic electron transport and anaerobic metabolism in purple non-sulfur phototrophic bacteria. Anton. Leeuw. 66, 151-164.
    • (1994) Anton. Leeuw. , vol.66 , pp. 151-164
    • McEwan, A.G.1
  • 15
    • 0000355874 scopus 로고
    • Identification of cytochromes involved in the electron transport to trimethylamine N-oxide / dimethylsulfoxide reductase in Rhodobacter capsulatus
    • McEwan, A.G., Richardson, DJ., Hudig, H., Ferguson, S.J., and Jackson, J.B. (1989). Identification of cytochromes involved in the electron transport to trimethylamine N-oxide / dimethylsulfoxide reductase in Rhodobacter capsulatus. Biochim. Biophys. Acta 973, 308-314.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 308-314
    • McEwan, A.G.1    Richardson, D.J.2    Hudig, H.3    Ferguson, S.J.4    Jackson, J.B.5
  • 17
    • 0026130546 scopus 로고
    • A regulatory mutant of trimethylamine N-oxid reductase of E. coli K-12
    • Pascal, M.C., Lepelletier, M., Giordano, G., and Chippaux, M. (1991). A regulatory mutant of trimethylamine N-oxid reductase of E. coli K-12. FEMS Microbiol Lett 78, 297-300.
    • (1991) FEMS Microbiol Lett , vol.78 , pp. 297-300
    • Pascal, M.C.1    Lepelletier, M.2    Giordano, G.3    Chippaux, M.4
  • 18
    • 0003903343 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 19
    • 0027976928 scopus 로고
    • The rational design of amino acid sequences by artificial neural networks and simulated molecular evolution: De novo design of an idealized leader peptidase cleavage site
    • Schneider, G., and Wrede, P. (1994). The rational design of amino acid sequences by artificial neural networks and simulated molecular evolution: De novo design of an idealized leader peptidase cleavage site. Biophys. J. 66, 335-344.
    • (1994) Biophys. J. , vol.66 , pp. 335-344
    • Schneider, G.1    Wrede, P.2
  • 20
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of Dimethyl sulfoxide reductase from Rhodobacter capsulatus at a 1.88 Â Resolution
    • Schneider, F.,. Löwe, J., Huber, R., Schindelin, H., Kisker, C., and Knäblein, J. (1996). Crystal structure of Dimethyl sulfoxide reductase from Rhodobacter capsulatus at a 1.88 Â Resolution. J. Mol. Biol. 263, 53-69.
    • (1996) J. Mol. Biol. , vol.263 , pp. 53-69
    • Schneider, F.1    Löwe, J.2    Huber, R.3    Schindelin, H.4    Kisker, C.5    Knäblein, J.6
  • 21
    • 0029159268 scopus 로고
    • Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides Dimethyl Sulfoxide Reductase
    • Schultz, B.E., Hille, R., and Holm, R.H. (1995). Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides Dimethyl Sulfoxide Reductase. J. Am. Chem. Soc. 7 77, 827-828.
    • (1995) J. Am. Chem. Soc. , vol.7 , Issue.77 , pp. 827-828
    • Schultz, B.E.1    Hille, R.2    Holm, R.H.3
  • 22
    • 0016154301 scopus 로고
    • The 3'-terminal sequence of Escherichia col 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites
    • Shine, J., and Dalgarno, L. (1974). The 3'-terminal sequence of Escherichia col 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Nat. Acad. Sci. USA 77, 1342-1346.
    • (1974) Proc. Nat. Acad. Sci. USA , vol.77 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 23
    • 0029394803 scopus 로고
    • Molybdenum cofactor biosynthesis: The A thalinana cDNAcnx7 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three E. coli proteins
    • Stallmeyer, B., Nerlich, A., Schiemann, J., Brinkmann, H., and Mendel, R.R. (1995). Molybdenum cofactor biosynthesis: The A thalinana cDNAcnx7 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three E. coli proteins. Plant J. 8, 751-762.
    • (1995) Plant J. , vol.8 , pp. 751-762
    • Stallmeyer, B.1    Nerlich, A.2    Schiemann, J.3    Brinkmann, H.4    Mendel, R.R.5
  • 24
    • 0020480282 scopus 로고
    • Characterization of translational initiation sites in E. coli
    • Stormo, G.D., Schneider, TD., and Gold, LM. (1982). Characterization of translational initiation sites in E. coli. Nucleic Acids Res. 10, 2971-2996.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 2971-2996
    • Stormo, G.D.1    Schneider, T.D.2    Gold, L.M.3
  • 25
    • 0021770334 scopus 로고
    • How signal sequences maintain cleavage specifity
    • Von Heijne, G. (1984). How signal sequences maintain cleavage specifity. J. Mol. Biol. 7 73, 243-251.
    • (1984) J. Mol. Biol. , vol.7 , Issue.73 , pp. 243-251
    • Von Heijne, G.1
  • 26
    • 0023928974 scopus 로고
    • Transcending the impenetrable: how proteins come to terms with membranes
    • Von Heijne, G. (1988). Transcending the impenetrable: how proteins come to terms with membranes. Biochim. Biophys. Acta 947, 307-333.
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 307-333
    • Von Heijne, G.1
  • 27
    • 0023110511 scopus 로고
    • The leader peptides from bacteriorhodopsin and halorhodopsin are potential membran-spanning amphipathic helices
    • Von Heijne, G., and Segrest, J. R.(1987). The leader peptides from bacteriorhodopsin and halorhodopsin are potential membran-spanning amphipathic helices. FEBS Lett. 273, 238-240.
    • (1987) FEBS Lett. , vol.273 , pp. 238-240
    • Von Heijne, G.1    Segrest, J.R.2
  • 28
    • 0011912247 scopus 로고
    • Characterization of Rhodobacter capsulata under anaerobic dark conditions with DMSO
    • Weaver. RF, Wall, J.D., and Gest, H. (1975a). Characterization of Rhodobacter capsulata under anaerobic dark conditions with DMSO. Arch. Bioch. Biophys. 787, 411-418.
    • (1975) Arch. Bioch. Biophys. , vol.787 , pp. 411-418
    • Weaver, R.F.1    Wall, J.D.2    Gest, H.3
  • 29
    • 0016720598 scopus 로고
    • Characterization of Rhodopseudomonas capsulata
    • Weaver, P. F., Wall, J.D., and Gest, H. (1975b). Characterization of Rhodopseudomonas capsulata. Arch. Microb. 105, 207-216.
    • (1975) Arch. Microb. , vol.105 , pp. 207-216
    • Weaver, P.F.1    Wall, J.D.2    Gest, H.3
  • 30
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-bind-ing domains
    • Wootton, J.C., Nicolson, R.E., Cock, J.M., Walters, D.E., Burke, J.R., Doyle, W.A., and Bray, R.C. (1991). Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-bind-ing domains. Biochim. Biophys. Acta 1057, 157-185.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 157-185
    • Wootton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.R.5    Doyle, W.A.6    Bray, R.C.7
  • 31
    • 0025848026 scopus 로고
    • Molybdenum requirement for translocation of dimethyl sulfoxide reductase to the periplasmic space in a photodenitrifier, Rhodobactersphaeroides f. sp. denitrificans
    • Yoshida, Y., Takai, M., Satoh, T., and Takami, S. (1991). Molybdenum requirement for translocation of dimethyl sulfoxide reductase to the periplasmic space in a photodenitrifier, Rhodobactersphaeroides f. sp. denitrificans. J. Bacterid. 7 73, 3277-3281.
    • (1991) J. Bacterid. , vol.7 , Issue.73 , pp. 3277-3281
    • Yoshida, Y.1    Takai, M.2    Satoh, T.3    Takami, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.