메뉴 건너뛰기




Volumn 185, Issue 1, 2003, Pages 107-114

Inactivation of the selB gene in Methanococcus maripaludis: Effect on synthesis of selenoproteins and their sulfur-containing homologs

Author keywords

[No Author keywords available]

Indexed keywords

SELENIUM DERIVATIVE; SELENOPROTEIN;

EID: 0037214551     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.1.107-114.2003     Document Type: Article
Times cited : (45)

References (37)
  • 3
    • 0025996978 scopus 로고
    • Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium
    • Axley, M. J., A. Böck, and T. C. Stadtman. 1991. Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium. Proc. Natl. Acad. Sci. USA 88:8450-8454.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8450-8454
    • Axley, M.J.1    Böck, A.2    Stadtman, T.C.3
  • 4
    • 0029072466 scopus 로고
    • Insertional mutations in the hydrogenase vhc and ftc operons encoding selenium free hydrogenases in Methanococcus voltae
    • Berghöfer, Y., and A. Klein. 1995. Insertional mutations in the hydrogenase vhc and ftc operons encoding selenium free hydrogenases in Methanococcus voltae. Appl. Environ. Microbiol. 61:1770-1775.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1770-1775
    • Berghöfer, Y.1    Klein, A.2
  • 5
    • 0025777391 scopus 로고
    • Evidence that cysteine, not selenocysteine, is in the catalytic site of type II iodothyronine deiodinase
    • Berry, M. J., J. D. Kieffer, and P. R. Larsen. 1991. Evidence that cysteine, not selenocysteine, is in the catalytic site of type II iodothyronine deiodinase. Endocrinology 129:550-552.
    • (1991) Endocrinology , vol.129 , pp. 550-552
    • Berry, M.J.1    Kieffer, J.D.2    Larsen, P.R.3
  • 7
    • 0031019644 scopus 로고    scopus 로고
    • Transcriptional regulation in Archaea: In vivo demonstration of a repressor binding site in a methanogen
    • Cohen-Kupiec, R., C. Blank, and J. A. Leigh. 1997. Transcriptional regulation in Archaea: In vivo demonstration of a repressor binding site in a methanogen. Proc. Natl. Acad. Sci. USA 94:1316-1320.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1316-1320
    • Cohen-Kupiec, R.1    Blank, C.2    Leigh, J.A.3
  • 8
    • 0033520423 scopus 로고    scopus 로고
    • Regulation of human thioredoxin reductase expression and activity by 3′-untranslated region selenocysteine insertion sequence and mRNA instability elements
    • Gasdaska, J. R., J. W. Harney, P. Y. Gasdaska, G. Powis, and M. J. Berry. 1999. Regulation of human thioredoxin reductase expression and activity by 3′-untranslated region selenocysteine insertion sequence and mRNA instability elements. J. Biol. Chem. 274:25379-25385.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25379-25385
    • Gasdaska, J.R.1    Harney, J.W.2    Gasdaska, P.Y.3    Powis, G.4    Berry, M.J.5
  • 9
    • 0025305971 scopus 로고
    • Construction of an integration vector for use in the archaebacterium Methanococcus voltae and expression of a eubacterial resistance gene
    • Gernhardt, P., O. Possot, M. Foglino, L. Sibold, and A. Klein. 1990. Construction of an integration vector for use in the archaebacterium Methanococcus voltae and expression of a eubacterial resistance gene. Mol. Gen. Genet. 221:273-279.
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 273-279
    • Gernhardt, P.1    Possot, O.2    Foglino, M.3    Sibold, L.4    Klein, A.5
  • 10
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg, A., W. Postel, and S. Gunther. 1988. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9:531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Görg, A.1    Postel, W.2    Gunther, S.3
  • 11
    • 0012125328 scopus 로고
    • Redox enzymes of methanogens: Physicochemical properties of selected purified oxidoreductases
    • J. G. Ferry (ed.). Chapman & Hall, London, England
    • Grahame, D. A., and T. C. Stadtman. 1993. Redox enzymes of methanogens: Physicochemical properties of selected purified oxidoreductases, p. 335-359. In J. G. Ferry (ed.), Methanogenesis. Chapman & Hall, London, England.
    • (1993) Methanogenesis , pp. 335-359
    • Grahame, D.A.1    Stadtman, T.C.2
  • 13
    • 0026564523 scopus 로고
    • Targeted insertion of selenocysteine into the alpha subunit of formate dehydrogenase from Metanobacterium formicicum
    • Heider, J., and A. Böck. 1992. Targeted insertion of selenocysteine into the alpha subunit of formate dehydrogenase from Metanobacterium formicicum. J. Bacteriol. 174:659-663.
    • (1992) J. Bacteriol. , vol.174 , pp. 659-663
    • Heider, J.1    Böck, A.2
  • 14
    • 0019497185 scopus 로고
    • Selenium-dependent and seleniumin-dependent formate dehydrogenases of Methanococcus vannielii: Separation of the two forms and characterization of the purified selenium-independent form
    • Jones, J. B., and T. C. Stadtman. 1981. Selenium-dependent and seleniumin-dependent formate dehydrogenases of Methanococcus vannielii: Separation of the two forms and characterization of the purified selenium-independent form. J. Biol. Chem. 256:656-663.
    • (1981) J. Biol. Chem. , vol.256 , pp. 656-663
    • Jones, J.B.1    Stadtman, T.C.2
  • 15
    • 0002620715 scopus 로고
    • Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment
    • Jones, W. J., M. J. B. Paynter, and R. Gupta. 1983. Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment. Arch. Microbiol. 135:91-97.
    • (1983) Arch. Microbiol. , vol.135 , pp. 91-97
    • Jones, W.J.1    Paynter, M.J.B.2    Gupta, R.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
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer, J., H. C. Kuettner, J. K. Zhang, R. Hedderich, and W. W. Metcalf. 2002. Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc. Natl. Acad. Sci. USA 99:5632-5637.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.W.5
  • 18
    • 0034917831 scopus 로고    scopus 로고
    • Coordinate positive regulation of genes encoding [NiFe] hydrogenases in Methanococcus voltae
    • Müller, S., and A. Klein. 2001. Coordinate positive regulation of genes encoding [NiFe] hydrogenases in Methanococcus voltae. Mol. Genet. Genomics 265:1069-1075.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 1069-1075
    • Müller, S.1    Klein, A.2
  • 19
    • 0035015556 scopus 로고    scopus 로고
    • Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region
    • Rother, M., A. Resch, W. L. Gardner, W. B. Whitman, and A. Böck. 2001. Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region. Mol. Microbiol. 40:900-908.
    • (2001) Mol. Microbiol. , vol.40 , pp. 900-908
    • Rother, M.1    Resch, A.2    Gardner, W.L.3    Whitman, W.B.4    Böck, A.5
  • 21
    • 0034595505 scopus 로고    scopus 로고
    • Identification and characterisation of the selenocysteine-specific translation factor SelB from the archaeon Methanococcus jannaschii
    • Rother, M., R. Wilting, S. Commans, and A. Böck. 2000. Identification and characterisation of the selenocysteine-specific translation factor SelB from the archaeon Methanococcus jannaschii. J. Mol. Biol. 299:351-358.
    • (2000) J. Mol. Biol. , vol.299 , pp. 351-358
    • Rother, M.1    Wilting, R.2    Commans, S.3    Böck, A.4
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 24
    • 0022558376 scopus 로고
    • 420-dependent formate dehydrogenase from Methanobacterium formicicum
    • 420-dependent formate dehydrogenase from Methanobacterium formicicum. J. Bacteriol. 165:405-411.
    • (1986) J. Bacteriol. , vol.165 , pp. 405-411
    • Schauer, N.L.1    Ferry, J.G.2
  • 25
    • 0021275385 scopus 로고
    • Immunoblotting analysis of ribosomal proteins from archaebacteria
    • Schmid, G., and A. Böck. 1984. Immunoblotting analysis of ribosomal proteins from archaebacteria. Syst. Appl. Microbiol. 5:1-10.
    • (1984) Syst. Appl. Microbiol. , vol.5 , pp. 1-10
    • Schmid, G.1    Böck, A.2
  • 26
    • 0022885197 scopus 로고
    • Cloning, expression, and nucleotide sequence of the formate dehydrogenase genes from Methanobacterium formicicum
    • Shuber, A. P., E. C. Orr, M. A. Recny, P. F. Schendel, H. D. May, N. L. Schauer, and J. G. Ferry. 1986. Cloning, expression, and nucleotide sequence of the formate dehydrogenase genes from Methanobacterium formicicum. J. Biol. Chem. 261:12942-12947.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12942-12947
    • Shuber, A.P.1    Orr, E.C.2    Recny, M.A.3    Schendel, P.F.4    May, H.D.5    Schauer, N.L.6    Ferry, J.G.7
  • 27
    • 0030957417 scopus 로고    scopus 로고
    • The [NiFe] hydrogenases of Methanococcus voltae: Genes, enzymes and regulation
    • Sorgenfrei, O., S. Müller, M. Pfeiffer, I. Sniezko, and A. Klein. 1997. The [NiFe] hydrogenases of Methanococcus voltae: Genes, enzymes and regulation. Arch. Microbiol. 167:189-195.
    • (1997) Arch. Microbiol. , vol.167 , pp. 189-195
    • Sorgenfrei, O.1    Müller, S.2    Pfeiffer, M.3    Sniezko, I.4    Klein, A.5
  • 28
    • 0023598337 scopus 로고
    • Specific occurrence of selenium in enzymes and amino acid tRNAs
    • Stadtman, T. C. 1987. Specific occurrence of selenium in enzymes and amino acid tRNAs. FASEB J. 1:375-379.
    • (1987) FASEB J. , vol.1 , pp. 375-379
    • Stadtman, T.C.1
  • 31
    • 0002867760 scopus 로고
    • Growth of methanogens on solidified medium
    • K. R. Sowers and H. J. Schreier ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Tumbula, D. L., T. L. Bowen, and W. B. Whitman. 1995. Growth of methanogens on solidified medium, p. 49-55. In K. R. Sowers and H. J. Schreier ed.), Archaea: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1995) Archaea: A Laboratory Manual , pp. 49-55
    • Tumbula, D.L.1    Bowen, T.L.2    Whitman, W.B.3
  • 32
    • 0028168940 scopus 로고
    • Transformation of Methanococcus maripaludis and identification of a PstI-like restriction system
    • Tumbula, D. L., T. L. Bowen, and W. B. Whitman. 1994. Transformation of Methanococcus maripaludis and identification of a PstI-like restriction system. FEMS Microbiol. Lett. 121:309-314.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 309-314
    • Tumbula, D.L.1    Bowen, T.L.2    Whitman, W.B.3
  • 33
    • 0032970932 scopus 로고    scopus 로고
    • Genetics of Methanococcus: Possibilities for functional genomics in Archaea
    • Tumbula, D. L., and W. B. Whitman. 1999. Genetics of Methanococcus: Possibilities for functional genomics in Archaea. Mol. Microbiol 33:1-7.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1-7
    • Tumbula, D.L.1    Whitman, W.B.2
  • 34
    • 0031017621 scopus 로고    scopus 로고
    • A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri
    • Vorholt, J. A., M. Vaupel, and R. K. Thauer. 1997. A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri. Mol. Microbiol. 23:1033-1042.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1033-1042
    • Vorholt, J.A.1    Vaupel, M.2    Thauer, R.K.3
  • 35
    • 0031320051 scopus 로고    scopus 로고
    • Preliminary investigation of tRNA modification enzymes with Se in bovine liver
    • Watanabe, T., K. Kanaya, T. Fujiwara, and T. Mizutani. 1997. Preliminary investigation of tRNA modification enzymes with Se in bovine liver. Nucleic Acids Symp. Ser. 37:155-156.
    • (1997) Nucleic Acids Symp. Ser. , vol.37 , pp. 155-156
    • Watanabe, T.1    Kanaya, K.2    Fujiwara, T.3    Mizutani, T.4
  • 37
    • 0031557397 scopus 로고    scopus 로고
    • Selenoprotein synthesis in Archaea: Identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion
    • Wilting, R., S. Schorling, B. C. Persson, and A. Böck. 1997. Selenoprotein synthesis in Archaea: Identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion. J. Mol. Biol. 266:637-641.
    • (1997) J. Mol. Biol. , vol.266 , pp. 637-641
    • Wilting, R.1    Schorling, S.2    Persson, B.C.3    Böck, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.