메뉴 건너뛰기




Volumn 81, Issue 1, 2011, Pages 249-258

Genetic analysis of selenocysteine biosynthesis in the archaeon Methanococcus maripaludis

Author keywords

[No Author keywords available]

Indexed keywords

CARBON DIOXIDE; FORMIC ACID; HYDROGEN; HYDROGENASE; PHOSPHOSERYL TRANSFER RNA KINASE; PHOSPHOTRANSFERASE; PROTEIN FRC; PROTEIN VHC; SELENIUM; SELENOCYSTEINE; SELENOPHOSPHATE SYNTHETASE; SERINE TRANSFER RNA; SERINE TRANSFER RNA LIGASE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 79959553087     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07690.x     Document Type: Article
Times cited : (17)

References (49)
  • 1
    • 65249146135 scopus 로고    scopus 로고
    • The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes
    • Aeby, E., Palioura, S., Pusnik, M., Marazzi, J., Lieberman, A., Ullu, E., etal. (2009) The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes. Proc Natl Acad Sci USA 106: 5088-5092.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5088-5092
    • Aeby, E.1    Palioura, S.2    Pusnik, M.3    Marazzi, J.4    Lieberman, A.5    Ullu, E.6
  • 2
    • 40249116863 scopus 로고    scopus 로고
    • Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation
    • Araiso, Y., Palioura, S., Ishitani, R., Sherrer, R.L., O'Donoghue, P., Yuan, J., etal. (2008) Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation. Nucleic Acids Res 36: 1187-1199.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1187-1199
    • Araiso, Y.1    Palioura, S.2    Ishitani, R.3    Sherrer, R.L.4    O'Donoghue, P.5    Yuan, J.6
  • 3
    • 0029804967 scopus 로고    scopus 로고
    • Neomycin resistance as a selectable marker in Methanococcus maripaludis
    • Argyle, J.L., Tumbula, D.L., and Leigh, J.A. (1996) Neomycin resistance as a selectable marker in Methanococcus maripaludis. Appl Environ Microbiol 62: 4233-4237.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4233-4237
    • Argyle, J.L.1    Tumbula, D.L.2    Leigh, J.A.3
  • 4
    • 0025996978 scopus 로고
    • Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium
    • Axley, M.J., Böck, A., and Stadtman, T.C. (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
  • 6
    • 0028198145 scopus 로고
    • Selenium is involved in the negative regulation of the expression of selenium-free [NiFe] hydrogenases in Methanococcus voltae
    • Berghöfer, Y., Agha-Amiri, K., and Klein, A. (1994) Selenium is involved in the negative regulation of the expression of selenium-free [NiFe] hydrogenases in Methanococcus voltae. Mol Gen Genet 242: 369-373.
    • (1994) Mol Gen Genet , vol.242 , pp. 369-373
    • Berghöfer, Y.1    Agha-Amiri, K.2    Klein, A.3
  • 7
    • 0025743489 scopus 로고
    • Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region
    • Berry, M.J., Banu, L., Chen, Y.Y., Mandel, S.J., Kieffer, J.D., Harney, J.W., and Larsen, P.R. (1991) Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region. Nature 353: 273-276.
    • (1991) Nature , vol.353 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Chen, Y.Y.3    Mandel, S.J.4    Kieffer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 8
    • 0028785817 scopus 로고
    • Genetics in methanogens: transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene
    • Blank, C.E., Kessler, P.S., and Leigh, J.A. (1995) Genetics in methanogens: transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene. J Bacteriol 177: 5773-5777.
    • (1995) J Bacteriol , vol.177 , pp. 5773-5777
    • Blank, C.E.1    Kessler, P.S.2    Leigh, J.A.3
  • 9
    • 4344682733 scopus 로고    scopus 로고
    • Selenocysteine
    • Ibba, M., Francklyn, C.S., and Cusack, S. (eds). Georgetown, Washington, DC: Landes Bioscience
    • Böck, A., Thanbichler, M., Rother, M., and Resch, A. (2005) Selenocysteine. In Aminoacyl-tRNA Synthetases. Ibba, M., Francklyn, C.S., and Cusack, S. (eds). Georgetown, Washington, DC: Landes Bioscience, pp. 320-327.
    • (2005) Aminoacyl-tRNA Synthetases , pp. 320-327
    • Böck, A.1    Thanbichler, M.2    Rother, M.3    Resch, A.4
  • 11
    • 35448929983 scopus 로고    scopus 로고
    • Systematic deletion analyses of the fla genes in the flagella operon identify several genes essential for proper assembly and function of flagella in the archaeon, Methanococcus maripaludis
    • Chaban, B., Ng, S.Y., Kanbe, M., Saltzman, I., Nimmo, G., Aizawa, S., and Jarrell, K.F. (2007) Systematic deletion analyses of the fla genes in the flagella operon identify several genes essential for proper assembly and function of flagella in the archaeon, Methanococcus maripaludis. Mol Microbiol 66: 596-609.
    • (2007) Mol Microbiol , vol.66 , pp. 596-609
    • Chaban, B.1    Ng, S.Y.2    Kanbe, M.3    Saltzman, I.4    Nimmo, G.5    Aizawa, S.6    Jarrell, K.F.7
  • 12
    • 0029065955 scopus 로고
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158: 9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 13
    • 0021140102 scopus 로고
    • Occurrence of selenium-containing tRNAs in mouse leukemia cells
    • Ching, W.M. (1984) Occurrence of selenium-containing tRNAs in mouse leukemia cells. Proc Natl Acad Sci USA 81: 3010-3013.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3010-3013
    • Ching, W.M.1
  • 14
    • 0021344872 scopus 로고
    • Distribution of two selenonucleosides among the selenium-containing tRNAs from Methanococcus vannielii
    • Ching, W.M., Wittwer, A.J., Tsai, L., and Stadtman, T.C. (1984) Distribution of two selenonucleosides among the selenium-containing tRNAs from Methanococcus vannielii. Proc Natl Acad Sci USA 81: 57-60.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 57-60
    • Ching, W.M.1    Wittwer, A.J.2    Tsai, L.3    Stadtman, T.C.4
  • 16
    • 0029988995 scopus 로고    scopus 로고
    • A modular set of Flp, FRT and lacZ fusion vectors for manipulating genes by site-specific recombination
    • Dymecki, S.M. (1996) A modular set of Flp, FRT and lacZ fusion vectors for manipulating genes by site-specific recombination. Gene 171: 197-201.
    • (1996) Gene , vol.171 , pp. 197-201
    • Dymecki, S.M.1
  • 17
    • 0034282536 scopus 로고    scopus 로고
    • Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation
    • Fagegaltier, D., Hubert, N., Yamada, K., Mizutani, T., Carbon, P., and Krol, A. (2000) Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation. EMBO J 19: 4796-4805.
    • (2000) EMBO J , vol.19 , pp. 4796-4805
    • Fagegaltier, D.1    Hubert, N.2    Yamada, K.3    Mizutani, T.4    Carbon, P.5    Krol, A.6
  • 18
    • 0015880169 scopus 로고
    • Glutathione peroxidase: a selenoenzyme
    • Flohe, L., Gunzler, W.A., and Schock, H.H. (1973) Glutathione peroxidase: a selenoenzyme. FEBS Lett 32: 132-134.
    • (1973) FEBS Lett , vol.32 , pp. 132-134
    • Flohe, L.1    Gunzler, W.A.2    Schock, H.H.3
  • 19
    • 0025736565 scopus 로고
    • Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence
    • Forchhammer, K., and Böck, A. (1991) Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence. J Biol Chem 266: 6324-6328.
    • (1991) J Biol Chem , vol.266 , pp. 6324-6328
    • Forchhammer, K.1    Böck, A.2
  • 20
    • 0024420343 scopus 로고
    • Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein
    • Forchhammer, K., Leinfelder, W., and Böck, A. (1989) Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. Nature 342: 453-456.
    • (1989) Nature , vol.342 , pp. 453-456
    • Forchhammer, K.1    Leinfelder, W.2    Böck, A.3
  • 21
    • 4944254822 scopus 로고    scopus 로고
    • Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis
    • Hendrickson, E.L., Kaul, R., Zhou, Y., Bovee, D., Chapman, P., Chung, J., etal. (2004) Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis. J Bacteriol 186: 6956-6969.
    • (2004) J Bacteriol , vol.186 , pp. 6956-6969
    • Hendrickson, E.L.1    Kaul, R.2    Zhou, Y.3    Bovee, D.4    Chapman, P.5    Chung, J.6
  • 22
    • 78751525775 scopus 로고    scopus 로고
    • Genome copy numbers and gene conversion in methanogenic archaea
    • Hildenbrand, C., Stock, T., Lange, C., Rother, M., and Soppa, J. (2011) Genome copy numbers and gene conversion in methanogenic archaea. J Bacteriol 193: 734-743.
    • (2011) J Bacteriol , vol.193 , pp. 734-743
    • Hildenbrand, C.1    Stock, T.2    Lange, C.3    Rother, M.4    Soppa, J.5
  • 23
    • 26444613250 scopus 로고    scopus 로고
    • Structural and functional investigation of a putative archaeal selenocysteine synthase
    • Kaiser, J.T., Gromadski, K., Rother, M., Engelhardt, H., Rodnina, M.V., and Wahl, M.C. (2005) Structural and functional investigation of a putative archaeal selenocysteine synthase. Biochemistry 44: 13315-13327.
    • (2005) Biochemistry , vol.44 , pp. 13315-13327
    • Kaiser, J.T.1    Gromadski, K.2    Rother, M.3    Engelhardt, H.4    Rodnina, M.V.5    Wahl, M.C.6
  • 24
    • 2942546160 scopus 로고    scopus 로고
    • The prokaryotic selenoproteome
    • Kryukov, G.V., and Gladyshev, V.N. (2004) The prokaryotic selenoproteome. EMBO Rep 5: 538-543.
    • (2004) EMBO Rep , vol.5 , pp. 538-543
    • Kryukov, G.V.1    Gladyshev, V.N.2
  • 25
    • 0025056970 scopus 로고
    • In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product
    • Leinfelder, W., Forchhammer, K., Veprek, B., Zehelein, E., and Böck, A. (1990) In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product. Proc Natl Acad Sci USA 87: 543-547.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 543-547
    • Leinfelder, W.1    Forchhammer, K.2    Veprek, B.3    Zehelein, E.4    Böck, A.5
  • 26
    • 0029812493 scopus 로고    scopus 로고
    • FLP-mediated recombination of FRT sites in the maize genome
    • Lyznik, L.A., Rao, K.V., and Hodges, T.K. (1996) FLP-mediated recombination of FRT sites in the maize genome. Nucleic Acids Res 24: 3784-3789.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3784-3789
    • Lyznik, L.A.1    Rao, K.V.2    Hodges, T.K.3
  • 27
    • 13244269794 scopus 로고    scopus 로고
    • Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease
    • Moore, B.C., and Leigh, J.A. (2005) Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease. J Bacteriol 187: 972-979.
    • (2005) J Bacteriol , vol.187 , pp. 972-979
    • Moore, B.C.1    Leigh, J.A.2
  • 28
    • 27844514673 scopus 로고    scopus 로고
    • Genetic technologies for Archaea
    • Rother, M., and Metcalf, W.W. (2005) Genetic technologies for Archaea. Curr Opin Microbiol 8: 745-751.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 745-751
    • Rother, M.1    Metcalf, W.W.2
  • 30
    • 0037214551 scopus 로고    scopus 로고
    • Inactivation of the selB gene in Methanococcus maripaludis: effect on synthesis of selenoproteins and their sulfur-containing homologs
    • Rother, M., Mathes, I., Lottspeich, F., and Böck, A. (2003) Inactivation of the selB gene in Methanococcus maripaludis: effect on synthesis of selenoproteins and their sulfur-containing homologs. J Bacteriol 185: 107-114.
    • (2003) J Bacteriol , vol.185 , pp. 107-114
    • Rother, M.1    Mathes, I.2    Lottspeich, F.3    Böck, A.4
  • 32
    • 0028843052 scopus 로고
    • The Flp recombinase of the 2-microns plasmid of Saccharomyces cerevisiae
    • Sadowski, P.D. (1995) The Flp recombinase of the 2-microns plasmid of Saccharomyces cerevisiae. Prog Nucleic Acid Res Mol Biol 51: 53-91.
    • (1995) Prog Nucleic Acid Res Mol Biol , vol.51 , pp. 53-91
    • Sadowski, P.D.1
  • 33
    • 0025856535 scopus 로고
    • Recovery of an integration shuttle vector from tandem repeats in Methanococcus maripaludis
    • Sandbeck, K.A., and Leigh, J.A. (1991) Recovery of an integration shuttle vector from tandem repeats in Methanococcus maripaludis. Appl Environ Microbiol 57: 2762-2763.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 2762-2763
    • Sandbeck, K.A.1    Leigh, J.A.2
  • 35
    • 0042196461 scopus 로고    scopus 로고
    • Applications of the Saccharomyces cerevisiae Flp-FRT system in bacterial genetics
    • Schweizer, H.P. (2003) Applications of the Saccharomyces cerevisiae Flp-FRT system in bacterial genetics. J Mol Microbiol Biotechnol 5: 67-77.
    • (2003) J Mol Microbiol Biotechnol , vol.5 , pp. 67-77
    • Schweizer, H.P.1
  • 37
    • 40249116860 scopus 로고    scopus 로고
    • Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation
    • Sherrer, R.L., O'Donoghue, P., and Söll, D. (2008b) Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation. Nucleic Acids Res 36: 1247-1259.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1247-1259
    • Sherrer, R.L.1    O'Donoghue, P.2    Söll, D.3
  • 38
    • 0035807913 scopus 로고    scopus 로고
    • Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis
    • Stathopoulos, C., Kim, W., Li, T., Anderson, I., Deutsch, B., Palioura, S., etal. (2001) Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis. Proc Natl Acad Sci USA 98: 14292-14297.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14292-14297
    • Stathopoulos, C.1    Kim, W.2    Li, T.3    Anderson, I.4    Deutsch, B.5    Palioura, S.6
  • 39
    • 72949104139 scopus 로고    scopus 로고
    • In vivo requirement of selenophosphate for selenoprotein synthesis in archaea
    • Stock, T., Selzer, M., and Rother, M. (2010) In vivo requirement of selenophosphate for selenoprotein synthesis in archaea. Mol Microbiol 75: 149-160.
    • (2010) Mol Microbiol , vol.75 , pp. 149-160
    • Stock, T.1    Selzer, M.2    Rother, M.3
  • 40
    • 1942436905 scopus 로고    scopus 로고
    • A lysR-type regulator is involved in the negative regulation of genes encoding selenium-free hydrogenases in the archaeon Methanococcus voltae
    • Sun, J., and Klein, A. (2004) A lysR-type regulator is involved in the negative regulation of genes encoding selenium-free hydrogenases in the archaeon Methanococcus voltae. Mol Microbiol 52: 563-571.
    • (2004) Mol Microbiol , vol.52 , pp. 563-571
    • Sun, J.1    Klein, A.2
  • 41
    • 0028168940 scopus 로고
    • Transformation of Methanococcus maripaludis and identification of a Pst I-like restriction system
    • Tumbula, D.L., Makula, R.A., and Whitman, W.B. (1994) Transformation of Methanococcus maripaludis and identification of a Pst I-like restriction system. FEMS Microbiol Lett 121: 309-314.
    • (1994) FEMS Microbiol Lett , vol.121 , pp. 309-314
    • Tumbula, D.L.1    Makula, R.A.2    Whitman, W.B.3
  • 42
    • 65349147066 scopus 로고    scopus 로고
    • Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis
    • VanDyke, D.J., Wu, J., Logan, S.M., Kelly, J.F., Mizuno, S., Aizawa, S., and Jarrell, K.F. (2009) Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis. Mol Microbiol 72: 633-644.
    • (2009) Mol Microbiol , vol.72 , pp. 633-644
    • VanDyke, D.J.1    Wu, J.2    Logan, S.M.3    Kelly, J.F.4    Mizuno, S.5    Aizawa, S.6    Jarrell, K.F.7
  • 43
    • 40449083311 scopus 로고    scopus 로고
    • Mutagenesis of the C1 oxidation pathway in Methanosarcina barkeri: new insights into the Mtr/Mer bypass pathway
    • Welander, P.V., and Metcalf, W.W. (2008) Mutagenesis of the C1 oxidation pathway in Methanosarcina barkeri: new insights into the Mtr/Mer bypass pathway. J Bacteriol 190: 1928-1936.
    • (2008) J Bacteriol , vol.190 , pp. 1928-1936
    • Welander, P.V.1    Metcalf, W.W.2
  • 44
    • 0030800138 scopus 로고    scopus 로고
    • Development of genetic approaches for the methane-producing archaebacterium Methanococcus maripaludis
    • Whitman, W.B., Tumbula, D.L., Yu, J.P., and Kim, W. (1997) Development of genetic approaches for the methane-producing archaebacterium Methanococcus maripaludis. Biofactors 6: 37-46.
    • (1997) Biofactors , vol.6 , pp. 37-46
    • Whitman, W.B.1    Tumbula, D.L.2    Yu, J.P.3    Kim, W.4
  • 45
    • 0021112373 scopus 로고
    • Specific incorporation of selenium into lysine- and glutamate-accepting tRNAs from Escherichia coli
    • Wittwer, A.J. (1983) Specific incorporation of selenium into lysine- and glutamate-accepting tRNAs from Escherichia coli. J Biol Chem 258: 8637-8641.
    • (1983) J Biol Chem , vol.258 , pp. 8637-8641
    • Wittwer, A.J.1
  • 46
    • 0037386409 scopus 로고    scopus 로고
    • Function and regulation of the formate dehydrogenase genes of the methanogenic archaeon Methanococcus maripaludis
    • Wood, G.E., Haydock, A.K., and Leigh, J.A. (2003) Function and regulation of the formate dehydrogenase genes of the methanogenic archaeon Methanococcus maripaludis. J Bacteriol 185: 2548-2554.
    • (2003) J Bacteriol , vol.185 , pp. 2548-2554
    • Wood, G.E.1    Haydock, A.K.2    Leigh, J.A.3
  • 48
    • 33845763611 scopus 로고    scopus 로고
    • RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea
    • Yuan, J., Palioura, S., Salazar, J.C., Su, D., O'Donoghue, P., Hohn, M.J., etal. (2006) RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc Natl Acad Sci USA 103: 18923-18927.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18923-18927
    • Yuan, J.1    Palioura, S.2    Salazar, J.C.3    Su, D.4    O'Donoghue, P.5    Hohn, M.J.6
  • 49
    • 77953707932 scopus 로고    scopus 로고
    • A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli
    • Yuan, J., Hohn, M.J., Sherrer, R.L., Palioura, S., Su, D., and Söll, D. (2010) A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli. FEBS Lett 584: 2857-2861.
    • (2010) FEBS Lett , vol.584 , pp. 2857-2861
    • Yuan, J.1    Hohn, M.J.2    Sherrer, R.L.3    Palioura, S.4    Su, D.5    Söll, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.