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Volumn 162, Issue 2, 2008, Pages 165-171

Selenocysteine incorporation in Kinetoplastid: Selenophosphate synthetase (SELD) from Leishmania major and Trypanosoma brucei

Author keywords

Leishmania; selD; Selenocysteine; Selenophosphate synthetase; Trypanosoma

Indexed keywords

SELENOCYSTEINE; SELENOPHOSPHATE SYNTHETASE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 54049091075     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2008.08.009     Document Type: Article
Times cited : (27)

References (33)
  • 1
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene
    • Gladyshev V.N., Jeang K.T., and Stadtman T.C. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci USA 93 (1996) 6146-6151
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.T.2    Stadtman, T.C.3
  • 4
    • 0035839432 scopus 로고    scopus 로고
    • Selenium metabolism in Drosophila: selenoproteins, selenoprotein mRNA expression, fertility, and mortality
    • Martin-Romero F.J., Kryukov G.V., Lobanov A.V., et al. Selenium metabolism in Drosophila: selenoproteins, selenoprotein mRNA expression, fertility, and mortality. J Biol Chem 276 (2001) 29798-29804
    • (2001) J Biol Chem , vol.276 , pp. 29798-29804
    • Martin-Romero, F.J.1    Kryukov, G.V.2    Lobanov, A.V.3
  • 5
    • 0001256080 scopus 로고
    • Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli
    • Zinoni F., Birkmann A., Stadtman T.C., and Bock A. Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc Natl Acad Sci USA 83 (1986) 4650-4654
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Bock, A.4
  • 7
    • 0041317009 scopus 로고    scopus 로고
    • Mechanism and regulation of selenoprotein synthesis
    • Driscoll D.M., and Copeland P.R. Mechanism and regulation of selenoprotein synthesis. Annu Rev Nutr 23 (2003) 17-40
    • (2003) Annu Rev Nutr , vol.23 , pp. 17-40
    • Driscoll, D.M.1    Copeland, P.R.2
  • 8
    • 0023907071 scopus 로고
    • Gene for a novel tRNA species that accepts l-serine and cotranslationally inserts selenocysteine
    • Leinfelder W., Zehelein E., Mandrand-Berthelot M.A., and Bock A. Gene for a novel tRNA species that accepts l-serine and cotranslationally inserts selenocysteine. Nature 331 (1988) 723-725
    • (1988) Nature , vol.331 , pp. 723-725
    • Leinfelder, W.1    Zehelein, E.2    Mandrand-Berthelot, M.A.3    Bock, A.4
  • 9
    • 0027144016 scopus 로고
    • Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX
    • Glass R.S., Singh W.P., Jung W., Veres Z., Scholz T.D., and Stadtman T.C. Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX. Biochemistry 32 (1993) 12555-12559
    • (1993) Biochemistry , vol.32 , pp. 12555-12559
    • Glass, R.S.1    Singh, W.P.2    Jung, W.3    Veres, Z.4    Scholz, T.D.5    Stadtman, T.C.6
  • 10
    • 0028289519 scopus 로고
    • Selenophosphate synthetase enzyme properties and catalytic reaction
    • Veres Z., Kim I.Y., Scholz T.D., and Stadtman T.C. Selenophosphate synthetase enzyme properties and catalytic reaction. J Biol Chem 269 (1994) 10597-10603
    • (1994) J Biol Chem , vol.269 , pp. 10597-10603
    • Veres, Z.1    Kim, I.Y.2    Scholz, T.D.3    Stadtman, T.C.4
  • 11
    • 0033524427 scopus 로고    scopus 로고
    • Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli
    • Lacourciere G.M., and Stadtman T.C. Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli. Proc Natl Acad Sci USA 96 (1999) 44-48
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 44-48
    • Lacourciere, G.M.1    Stadtman, T.C.2
  • 12
    • 33747795310 scopus 로고    scopus 로고
    • Identification of Leishmania selenoproteins and SECIS element
    • Cassago A., Rodrigues E.M., Prieto E.L., et al. Identification of Leishmania selenoproteins and SECIS element. Mol Biochem Parasitol 149 (2006) 128-134
    • (2006) Mol Biochem Parasitol , vol.149 , pp. 128-134
    • Cassago, A.1    Rodrigues, E.M.2    Prieto, E.L.3
  • 13
    • 33748537719 scopus 로고    scopus 로고
    • Selenium metabolism in Trypanosoma: characterization of selenoproteomes and identification of a kinetoplastida-specific selenoprotein
    • Lobanov A.V., Gromer S., Salinas G., and Gladyshev V.N. Selenium metabolism in Trypanosoma: characterization of selenoproteomes and identification of a kinetoplastida-specific selenoprotein. Nucleic Acids Res 34 (2006) 4012-4024
    • (2006) Nucleic Acids Res , vol.34 , pp. 4012-4024
    • Lobanov, A.V.1    Gromer, S.2    Salinas, G.3    Gladyshev, V.N.4
  • 14
    • 1642306973 scopus 로고    scopus 로고
    • The selenophosphate synthetase gene from Leishmania major
    • Jayakumar P.C., Musande V.V., Shouche Y.S., and Patole M.S. The selenophosphate synthetase gene from Leishmania major. DNA Seq 15 (2004) 66-70
    • (2004) DNA Seq , vol.15 , pp. 66-70
    • Jayakumar, P.C.1    Musande, V.V.2    Shouche, Y.S.3    Patole, M.S.4
  • 16
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0019551730 scopus 로고
    • "Western Blotting": eletrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette W.N. "Western Blotting": eletrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem 112 (1981) 195-203
    • (1981) Anal Biochem , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 20
    • 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 Bock A. 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 (1990) 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    Bock, A.5
  • 21
    • 0017841732 scopus 로고
    • Improved method for identification and characterization of mutants of Escherichia coli deficient in formate dehydrogenase-activity
    • Mandrandberthelot M.A., Wee M.Y.K., and Haddock B.A. Improved method for identification and characterization of mutants of Escherichia coli deficient in formate dehydrogenase-activity. FEMS Microbiol Lett 4 (1978) 37-40
    • (1978) FEMS Microbiol Lett , vol.4 , pp. 37-40
    • Mandrandberthelot, M.A.1    Wee, M.Y.K.2    Haddock, B.A.3
  • 22
    • 0037047140 scopus 로고    scopus 로고
    • Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteins
    • Lacourciere G.M., Levine R.L., and Stadtman T.C. Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteins. Proc Natl Acad Sci USA 99 (2002) 9150-9153
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9150-9153
    • Lacourciere, G.M.1    Levine, R.L.2    Stadtman, T.C.3
  • 24
    • 0032553428 scopus 로고    scopus 로고
    • The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate
    • Lacourciere G.M., and Stadtman T.C. The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate. J Biol Chem 273 (1998) 30921-30926
    • (1998) J Biol Chem , vol.273 , pp. 30921-30926
    • Lacourciere, G.M.1    Stadtman, T.C.2
  • 29
    • 9244265496 scopus 로고    scopus 로고
    • Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling l-selenocysteine and Sps2 for selenite assimilation
    • Tamura T., Yamamoto S., Takahata M., et al. Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling l-selenocysteine and Sps2 for selenite assimilation. Proc Natl Acad Sci USA 101 (2004) 16162-16167
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16162-16167
    • Tamura, T.1    Yamamoto, S.2    Takahata, M.3
  • 30
    • 0031557397 scopus 로고    scopus 로고
    • Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion
    • Wilting R., Schorling S., Persson B.C., and Bock A. Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion. J Mol Biol 266 (1997) 637-641
    • (1997) J Mol Biol , vol.266 , pp. 637-641
    • Wilting, R.1    Schorling, S.2    Persson, B.C.3    Bock, A.4
  • 31
    • 0026779417 scopus 로고
    • Escherichia coli mutant SELD enzymes the cysteine 17 residue is essential for selenophosphate formation from ATP and selenide
    • Kim I.Y., Veres Z., and Stadtman T.C. Escherichia coli mutant SELD enzymes the cysteine 17 residue is essential for selenophosphate formation from ATP and selenide. J Biol Chem 267 (1992) 19650-19654
    • (1992) J Biol Chem , vol.267 , pp. 19650-19654
    • Kim, I.Y.1    Veres, Z.2    Stadtman, T.C.3
  • 32
    • 18244430454 scopus 로고    scopus 로고
    • SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity
    • Persson B.C., Bock A., Jackle H., and Vorbruggen G. SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity. J Mol Biol 274 (1997) 174-180
    • (1997) J Mol Biol , vol.274 , pp. 174-180
    • Persson, B.C.1    Bock, A.2    Jackle, H.3    Vorbruggen, G.4
  • 33
    • 0001380812 scopus 로고
    • Formic dehydrogenase and the hydrogenlyase enzyme complex in Coli aerogenes bacteria
    • Peck Jr. H.D., and Gest H. Formic dehydrogenase and the hydrogenlyase enzyme complex in Coli aerogenes bacteria. J Bacteriol 73 (1957) 706-721
    • (1957) J Bacteriol , vol.73 , pp. 706-721
    • Peck Jr., H.D.1    Gest, H.2


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