메뉴 건너뛰기




Volumn 284, Issue 2, 1998, Pages 421-433

Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species

Author keywords

Anaerobiosis; C type cytochrome; Molybdoenzyme; Respiratory system; TMAO reductase

Indexed keywords

DIMETHYL SULFOXIDE; OXIDOREDUCTASE; TRIMETHYLAMINE; TRIMETHYLAMINE OXIDE;

EID: 0032573575     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2155     Document Type: Article
Times cited : (100)

References (49)
  • 1
    • 0026495435 scopus 로고
    • Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacteriumRoseobacter denitrificans
    • Arata H., Shimizu M., Takamiya K.I. Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacteriumRoseobacter denitrificans. J. Biochem. 112:1992;470-475
    • (1992) J. Biochem. , vol.112 , pp. 470-475
    • Arata, H.1    Shimizu, M.2    Takamiya, K.I.3
  • 2
    • 0021778428 scopus 로고
    • Bacterial reduction of trimethylamine oxide
    • Barrett E.L., Kwan H.S. Bacterial reduction of trimethylamine oxide. Annu. Rev. Microbiol. 39:1985;131-149
    • (1985) Annu. Rev. Microbiol. , vol.39 , pp. 131-149
    • Barrett, E.L.1    Kwan, H.S.2
  • 3
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for protein binding complex redox cofactors?
    • Berks B.C. A common export pathway for protein binding complex redox cofactors? Mol. Microbiol. 22:1996;393-404
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 4
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • Berks B.C., Ferguson S.J., Moir J.W.B., Richardson D.J. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta. 1232:1995;97-173
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 5
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethyl sulphoxide reductase of Escherichia coli
    • Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H. Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethyl sulphoxide reductase of Escherichia coli. Mol. Microbiol. 2:1988;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
  • 6
    • 0028061282 scopus 로고
    • Promoter structure, promoter recognition, and transcription activation in prokaryotes
    • Busby S., Ebright R.H. Promoter structure, promoter recognition, and transcription activation in prokaryotes. Cell. 79:1994;743-746
    • (1994) Cell , vol.79 , pp. 743-746
    • Busby, S.1    Ebright, R.H.2
  • 7
    • 0024296631 scopus 로고
    • A rapid and convenient method for the preparation and storage of competent bacterial cells
    • Chung C.T., Miller R.H. A rapid and convenient method for the preparation and storage of competent bacterial cells. Nucl. Acids Res. 16:1988;3580
    • (1988) Nucl. Acids Res. , vol.16 , pp. 3580
    • Chung, C.T.1    Miller, R.H.2
  • 8
    • 0003154369 scopus 로고
    • Purification and properties of trimethylamine N-oxide reductase from Shewanella sp. NCMB 400
    • Clarke G.J., Ward F.B. Purification and properties of trimethylamine N-oxide reductase from Shewanella sp. NCMB 400. J. Gen. Microbiol. 134:1988;379-386
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 379-386
    • Clarke, G.J.1    Ward, F.B.2
  • 9
    • 0032573427 scopus 로고    scopus 로고
    • Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 Å resolution
    • Czjzek M., Dos Santos J.P., Pommier J., Giordano G., Mëjean V., Haser R. Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 Å resolution. J. Mol. Biol. 284:1998;435-447
    • (1998) J. Mol. Biol. , vol.284 , pp. 435-447
    • Czjzek, M.1    Dos Santos, J.P.2    Pommier, J.3    Giordano, G.4    Mëjean, V.5    Haser, R.6
  • 10
    • 0021049657 scopus 로고
    • The induction and location of trimethylamine-N-oxyde reductase in Alteromonas sp. NCMB 400
    • Easter M.C., Gibson D.M., Ward F.B. The induction and location of trimethylamine-N-oxyde reductase in Alteromonas sp. NCMB 400. J. Gen. Microbiol. 129:1983;3689-3696
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 3689-3696
    • Easter, M.C.1    Gibson, D.M.2    Ward, F.B.3
  • 11
    • 0030297237 scopus 로고    scopus 로고
    • Microbiological spoilage of fish and fish products
    • Gram L., Huss H.H. Microbiological spoilage of fish and fish products. Int. J. Food Microbiol. 33:1996;121-137
    • (1996) Int. J. Food Microbiol. , vol.33 , pp. 121-137
    • Gram, L.1    Huss, H.H.2
  • 12
    • 0030014740 scopus 로고    scopus 로고
    • High substrate specificity and induction characteristics of trimethylamine N-oxide reductase of Escherichia coli
    • Iobbi-Nivol C., Pommier J., Simala-Grant J., Mëejean V., Giordano G. High substrate specificity and induction characteristics of trimethylamine N-oxide reductase of Escherichia coli. Biochim. Biophys. Acta. 1294:1996;77-82
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 77-82
    • Iobbi-Nivol, C.1    Pommier, J.2    Simala-Grant, J.3    Mëejean, V.4    Giordano, G.5
  • 13
    • 0028877781 scopus 로고
    • Conservation of cis-acting elements within the tor regulatory region among different Enterobacteriaceae
    • Jourlin C., Simon G., Lepelletier M., Chippaux M., Mëjean V. Conservation of cis-acting elements within the tor regulatory region among different Enterobacteriaceae. Gene. 152:1995;53-57
    • (1995) Gene , vol.152 , pp. 53-57
    • Jourlin, C.1    Simon, G.2    Lepelletier, M.3    Chippaux, M.4    Mëjean, V.5
  • 14
    • 0031564650 scopus 로고    scopus 로고
    • Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli
    • Jourlin C., Ansaldi M., Méjean V. Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli. J. Mol. Biol. 267:1997;770-777
    • (1997) J. Mol. Biol. , vol.267 , pp. 770-777
    • Jourlin, C.1    Ansaldi, M.2    Méjean, V.3
  • 15
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • H.N. Munro. New York: Academic Press
    • Jukes T.H., Cantor C.R. Evolution of protein molecules. Munro H.N. Mammalian Protein Metabolism. 1969;21-132 Academic Press, New York
    • (1969) Mammalian Protein Metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 16
    • 0030592480 scopus 로고    scopus 로고
    • Isolation, cloning, sequence analysis and localization of the operon encoding the dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus
    • Knäblein J., Mann K., Ehlert S., Fonstein M., Huber R., Schneider F. Isolation, cloning, sequence analysis and localization of the operon encoding the dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus. J. Mol. Biol. 263:1996;40-52
    • (1996) J. Mol. Biol. , vol.263 , pp. 40-52
    • Knäblein, J.1    Mann, K.2    Ehlert, S.3    Fonstein, M.4    Huber, R.5    Schneider, F.6
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0017596525 scopus 로고
    • A numerical taxonomic study of some pseudomonas-like marine bacteria
    • Lee J.V., Gibson D.M., Shewan J.M. A numerical taxonomic study of some pseudomonas-like marine bacteria. J. Gen. Microbiol. 98:1977;439-451
    • (1977) J. Gen. Microbiol. , vol.98 , pp. 439-451
    • Lee, J.V.1    Gibson, D.M.2    Shewan, J.M.3
  • 19
    • 0027230594 scopus 로고
    • Compilation of E. coli mRNA promoter sequences
    • Lisser S., Margalit H. Compilation of E. coli mRNA promoter sequences. Nucl. Acids Res. 21:1993;1507-1516
    • (1993) Nucl. Acids Res. , vol.21 , pp. 1507-1516
    • Lisser, S.1    Margalit, H.2
  • 24
    • 0025439406 scopus 로고
    • Influence of respiratory substrate on the cytochrome content of Shewanella putrefaciens
    • Morris C.J., Gibson D.M., Ward F.B. Influence of respiratory substrate on the cytochrome content of Shewanella putrefaciens. FEMS Microbiol. Letters. 69:1990;259-262
    • (1990) FEMS Microbiol. Letters , vol.69 , pp. 259-262
    • Morris, C.J.1    Gibson, D.M.2    Ward, F.B.3
  • 25
    • 0030835030 scopus 로고    scopus 로고
    • T an essential metabolic gene function encoded on chromosome II
    • T an essential metabolic gene function encoded on chromosome II. J. Bacteriol. 179:1997;7617-7624
    • (1997) J. Bacteriol. , vol.179 , pp. 7617-7624
    • Mouncey, N.J.1    Choudhary, M.2    Kaplan, S.3
  • 26
    • 0032568823 scopus 로고    scopus 로고
    • TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli
    • Pommier J., Méjean V., Giordano G., Iobbi-Nivol C. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli. J. Biol. Chem. 273:1998;16615-16620
    • (1998) J. Biol. Chem. , vol.273 , pp. 16615-16620
    • Pommier, J.1    Méjean, V.2    Giordano, G.3    Iobbi-Nivol, C.4
  • 27
    • 0029799968 scopus 로고    scopus 로고
    • The genus Nocardiopsis represents a phylogenetically coherent taxon and a distinct actinomycete lineage; Proposal of Nocardiopsaceae fam. nov
    • Rainey F.A., Ward-Rainey N., Kroppenstedt R.M., Stackebrandt E. The genus Nocardiopsis represents a phylogenetically coherent taxon and a distinct actinomycete lineage; proposal of Nocardiopsaceae fam. nov. Int. J. Sys. Bacteriol. 46:1996;1088-1092
    • (1996) Int. J. Sys. Bacteriol. , vol.46 , pp. 1088-1092
    • Rainey, F.A.1    Ward-Rainey, N.2    Kroppenstedt, R.M.3    Stackebrandt, E.4
  • 28
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 30
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini C.L., Ize B., Chanal A., Muller M., Giordano G., Wu L.F. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:1998;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
  • 31
    • 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. Crystal structure of DMSO reductase redox-linked changes in molybdopterin coordination. Science. 272:1996;1615-1621
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 32
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1. 88 Å resolution
    • Schneider F., Löwe J., Huber R., Schindelin H., Kisker C., Knäblein J. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1. 88 Å resolution. J. Mol. Biol. 263:1996;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
  • 33
    • 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. Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus. Biochim. Biophys. Acta. 1276:1996;176-180
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 176-180
    • Shaw, A.L.1    Hanson, G.R.2    McEwan, A.G.3
  • 34
    • 0024388691 scopus 로고
    • The inducible trimethylamine N-oxide reductase of Escherichia coli K12: Its localization and inducers
    • Silvestro A., Pommier J., Pascal M.C., Giordano G. The inducible trimethylamine N-oxide reductase of Escherichia coli K12 its localization and inducers. Biochim. Biophys. Acta. 999:1989;208-216
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 208-216
    • Silvestro, A.1    Pommier, J.2    Pascal, M.C.3    Giordano, G.4
  • 35
    • 0029854878 scopus 로고    scopus 로고
    • Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
    • Simala-Grant J.L., Weiner J.H. Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase. Microbiology. 142:1996;3231-3239
    • (1996) Microbiology , vol.142 , pp. 3231-3239
    • Simala-Grant, J.L.1    Weiner, J.H.2
  • 36
    • 0027959266 scopus 로고
    • The torR gene of Escherichia coli encodes a response regulator protein involved in the expression of the TMAO reductase genes
    • Simon G., Mëjean V., Jourlin C., Chippaux M., Pascal M.C. The torR gene of Escherichia coli encodes a response regulator protein involved in the expression of the TMAO reductase genes. J. Bacteriol. 176:1994;5601-5606
    • (1994) J. Bacteriol. , vol.176 , pp. 5601-5606
    • Simon, G.1    Mëjean, V.2    Jourlin, C.3    Chippaux, M.4    Pascal, M.C.5
  • 37
    • 0028862516 scopus 로고
    • Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression
    • Simon G., Jourlin C., Ansaldi M., Pascal M.C., Chippaux M., Mëjean V. Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression. Mol. Microbiol. 17:1995;971-980
    • (1995) Mol. Microbiol. , vol.17 , pp. 971-980
    • Simon, G.1    Jourlin, C.2    Ansaldi, M.3    Pascal, M.C.4    Chippaux, M.5    Mëjean, V.6
  • 39
    • 0021751994 scopus 로고
    • Dimethylsulphoxide and trimethylamine oxide respiration of Proteus vulgaris - Evidence for a common terminal reductase system
    • Styrvold O.B., Strom A.R. Dimethylsulphoxide and trimethylamine oxide respiration of Proteus vulgaris - evidence for a common terminal reductase system. Arch. Microbiol. 140:1984;74-78
    • (1984) Arch. Microbiol. , vol.140 , pp. 74-78
    • Styrvold, O.B.1    Strom, A.R.2
  • 40
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of the cytochrome P-450 on sodium dodecyl sulfate polyacrylamine gels
    • Thomas P.E., Ryan D., Levin W. An improved staining procedure for the detection of the peroxidase activity of the cytochrome P-450 on sodium dodecyl sulfate polyacrylamine gels. Anal. Biochem. 75:1976;168-176
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 41
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets procedure and some applications. Proc. Natl Acad. Sci. USA. 76:1979;4350-4354
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0029860353 scopus 로고    scopus 로고
    • Nucleotide sequence of the genes, encoding the pentahaem cytochrome (dmsC) and the transmembrane protein (dmsB), involved in dimethyl sulfoxide respiration from Rhodobacter sphaeroides f. sp denitrificans
    • Ujiiye T., Yamamoto I., Nakama H., Okudo A., Yamazaki S., Satoh T. Nucleotide sequence of the genes, encoding the pentahaem cytochrome (dmsC) and the transmembrane protein (dmsB), involved in dimethyl sulfoxide respiration from Rhodobacter sphaeroides f. sp denitrificans. Biochim. Biophys. Acta. 1277:1996;1-5
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 1-5
    • Ujiiye, T.1    Yamamoto, I.2    Nakama, H.3    Okudo, A.4    Yamazaki, S.5    Satoh, T.6
  • 43
    • 0030742434 scopus 로고    scopus 로고
    • The dmsR gene encoding a dimethyl sulfoxide-responsive regulator for expression of dmsCBA (dimethyl sulfoxide respiration genes) in Rhodobacter sphaeroides f. sp denitrificans
    • Ujiiye T., Yamamoto I., Satoh T. The dmsR gene encoding a dimethyl sulfoxide-responsive regulator for expression of dmsCBA (dimethyl sulfoxide respiration genes) in Rhodobacter sphaeroides f. sp denitrificans. Biochim. Biophys. Acta. 1353:1997;84-92
    • (1997) Biochim. Biophys. Acta , vol.1353 , pp. 84-92
    • Ujiiye, T.1    Yamamoto, I.2    Satoh, T.3
  • 44
    • 0013852731 scopus 로고
    • Intracellular localization and properties of trimethylamine-N-oxide reductase in Vibrio parahaemolyticus
    • Unemoto T., Hayashi M., Miyaki M. Intracellular localization and properties of trimethylamine-N-oxide reductase in Vibrio parahaemolyticus. Biochim. Biophys. Acta. 110:1965;319-328
    • (1965) Biochim. Biophys. Acta , vol.110 , pp. 319-328
    • Unemoto, T.1    Hayashi, M.2    Miyaki, M.3
  • 45
    • 0342941173 scopus 로고    scopus 로고
    • Differentiation of Shewanella putrefaciens and Shewanella alga on the basis of whole-cell protein profiles, ribotyping, phenotypic characterization, and 16 S rRNA gene sequence analysis
    • Vogel B.F., Jorgensen K., Christensen H., Olsen J.E., Gram L. Differentiation of Shewanella putrefaciens and Shewanella alga on the basis of whole-cell protein profiles, ribotyping, phenotypic characterization, and 16 S rRNA gene sequence analysis. Appl. Environ. Microbiol. 63:1997;2189-2199
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2189-2199
    • Vogel, B.F.1    Jorgensen, K.2    Christensen, H.3    Olsen, J.E.4    Gram, L.5
  • 46
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang A., Bolen D.W. A naturally occurring protective system in urea-rich cells mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry. 36:1997;9101-9108
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 49


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.