메뉴 건너뛰기




Volumn 18, Issue 8, 1999, Pages 2284-2293

Dynamics and efficiency in vivo of UGA-directed selenocysteine insertion at the ribosome

Author keywords

EF Tu; Ribosomal pausing; SelB; Selenocysteine; Translation efficiency

Indexed keywords

BETA GALACTOSIDASE; ELONGATION FACTOR TU; MESSENGER RNA; SELENOCYSTEINE; SELENOPROTEIN; SERINE TRANSFER RNA; TRANSFER RNA;

EID: 0033560765     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.8.2284     Document Type: Article
Times cited : (70)

References (52)
  • 1
    • 0027191822 scopus 로고
    • Gene expression in cell-free system on preparative scale
    • Baranov, V.I. and Spirin, A.S. (1993) Gene expression in cell-free system on preparative scale. Methods Enzymol., 217, 123-142.
    • (1993) Methods Enzymol. , vol.217 , pp. 123-142
    • Baranov, V.I.1    Spirin, A.S.2
  • 2
    • 0001314696 scopus 로고
    • The selenocysteine-inserting tRNA species: Structure and function
    • Söll, D. and RajBhandary, U.L. (eds), ASM Press, Washington, DC
    • Baron, C. and Böck, A. (1995) The selenocysteine-inserting tRNA species: structure and function. In Söll, D. and RajBhandary, U.L. (eds), tRNA: Structure, Biosynthesis and Function. ASM Press, Washington, DC, pp. 529-544.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 529-544
    • Baron, C.1    Böck, A.2
  • 3
    • 0025572409 scopus 로고
    • Mutagenesis of selC, the gene for the selenocysteine-inserting tRNA-species in E.coli: Effects on in vivo function
    • Baron, C., Heider, J. and Böck, A. (1990) Mutagenesis of selC, the gene for the selenocysteine-inserting tRNA-species in E.coli: effects on in vivo function. Nucleic Acids Res., 18, 6761-6766.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6761-6766
    • Baron, C.1    Heider, J.2    Böck, A.3
  • 4
    • 0027151982 scopus 로고
    • Interaction of translation factor SelB with the formate dehydrogenase selenopolypeptide mRNA
    • Baron, C., Heider, J. and Böck, A. (1993a) Interaction of translation factor SelB with the formate dehydrogenase selenopolypeptide mRNA. Proc. Natl Acad. Sci. USA, 90, 4181-4185.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4181-4185
    • Baron, C.1    Heider, J.2    Böck, A.3
  • 6
    • 0017389525 scopus 로고
    • The identification of mutants of Escherichia coli deficient in formate dehydrogenase aand nitrate reductase activities using dye indicator plates
    • Begg, Y.A., Whyte, J.N. and Haddock, B.A. (1977) The identification of mutants of Escherichia coli deficient in formate dehydrogenase aand nitrate reductase activities using dye indicator plates. FEMS Microbiol. Lett., 2, 47-50.
    • (1977) FEMS Microbiol. Lett. , vol.2 , pp. 47-50
    • Begg, Y.A.1    Whyte, J.N.2    Haddock, B.A.3
  • 8
    • 0026722791 scopus 로고
    • Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation
    • Berry, M.J., Maia, A.L., Kieffer, J.D., Harney, J.W. and Larsen, P.R. (1992) Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation. Endocrinology, 131, 1848-1852.
    • (1992) Endocrinology , vol.131 , pp. 1848-1852
    • Berry, M.J.1    Maia, A.L.2    Kieffer, J.D.3    Harney, J.W.4    Larsen, P.R.5
  • 9
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation of lysogeneic Escherichia coli
    • Bertani, G. (1951) Studies on lysogenesis. I. The mode of phage liberation of lysogeneic Escherichia coli. J. Bacteriol., 62, 293-300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 10
    • 0024280019 scopus 로고
    • Is translation inhibited by noncognate ternary complexes?
    • Bilgin, N., Ehrenberg, M. and Kurland, C. (1988) Is translation inhibited by noncognate ternary complexes? FEBS Lett., 233, 95-99.
    • (1988) FEBS Lett. , vol.233 , pp. 95-99
    • Bilgin, N.1    Ehrenberg, M.2    Kurland, C.3
  • 12
    • 0000640710 scopus 로고
    • Modification of chemical composition and other parameters of the cell by growth rate
    • Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M. and Umbarger, H.E. (eds), ASM Press, Washington, DC
    • Bremer, H. and Dennis, P.P. (1987) Modification of chemical composition and other parameters of the cell by growth rate. In Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M. and Umbarger, H.E. (eds), Escherichia coli and Salmonella typhimurium, Cellular and Molecular Biology. ASM Press, Washington, DC, pp. 1527-1542.
    • (1987) Escherichia Coli and Salmonella Typhimurium, Cellular and Molecular Biology , pp. 1527-1542
    • Bremer, H.1    Dennis, P.P.2
  • 13
    • 0000366608 scopus 로고
    • Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: In vivo probe for transcriptional control sequences
    • Casadaban, M.J. and Cohen, S.N. (1979) Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc. Natl Acad. Sci. USA, 76, 4530-4533.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4530-4533
    • Casadaban, M.J.1    Cohen, S.N.2
  • 14
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A.C.Y. and Cohen, S.N. (1978) Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol., 134, 1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 15
    • 0027486247 scopus 로고
    • Effect of the relative position of the UGA codon to the unique secondary structure in the fdhF mRNA on its decoding by selenocysteyl tRNA in Escherichia coli
    • Chen, G.-F.T., Fang, L. and Inouye, M. (1993) Effect of the relative position of the UGA codon to the unique secondary structure in the fdhF mRNA on its decoding by selenocysteyl tRNA in Escherichia coli. J. Biol. Chem., 268, 23128-23131.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23128-23131
    • Chen, G.-F.T.1    Fang, L.2    Inouye, M.3
  • 16
    • 0017606476 scopus 로고
    • Genetic studies of the lac repressor. III. Additional correlation of mutational sites with specific amino acid residues
    • Coulondre, C. and Miller, J.H. (1977) Genetic studies of the lac repressor. III. Additional correlation of mutational sites with specific amino acid residues. J. Mol. Biol., 117, 525-567.
    • (1977) J. Mol. Biol. , vol.117 , pp. 525-567
    • Coulondre, C.1    Miller, J.H.2
  • 17
    • 0019493806 scopus 로고
    • Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli
    • Cox, U.C., Edwards, E.S. and DeMoss, J.A. (1981) Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli. J. Bacteriol., 145, 1317-1324.
    • (1981) J. Bacteriol. , vol.145 , pp. 1317-1324
    • Cox, U.C.1    Edwards, E.S.2    Demoss, J.A.3
  • 18
    • 0030564828 scopus 로고    scopus 로고
    • Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates
    • Dong, H., Nilsson, L. and Kurland, C.G. (1996) Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates. J. Mol. Biol., 260, 649-663.
    • (1996) J. Mol. Biol. , vol.260 , pp. 649-663
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3
  • 19
    • 0030457112 scopus 로고    scopus 로고
    • Programmed translational frameshifting
    • Farabaugh, P.J. (1996) Programmed translational frameshifting. Annu. Rev. Genet., 30, 507-528.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 507-528
    • Farabaugh, P.J.1
  • 20
    • 0024420343 scopus 로고
    • Identification of a novel translation factor necessary for incorporation of selenocysteine into protein
    • Forchhammer, K., Leinfelder, W. and Böck, A. (1989) Identification of a novel translation factor necessary for 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
    • 0025291864 scopus 로고
    • Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis
    • Forchhammer, K., Rücknagel, K.P. and Böck, A. (1990) Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis. J. Biol. Chem., 265, 9346-9350.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9346-9350
    • Forchhammer, K.1    Rücknagel, K.P.2    Böck, A.3
  • 22
    • 0025103403 scopus 로고
    • Interaction of selenocysteine-incorporating tRNA with elongation factor Tu from E.coli
    • Förster, C., Ott, G., Forchhammer, K. and Sprinzl, M. (1990) Interaction of selenocysteine-incorporating tRNA with elongation factor Tu from E.coli. Nucleic Acids Res., 18, 487-491.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 487-491
    • Förster, C.1    Ott, G.2    Forchhammer, K.3    Sprinzl, M.4
  • 23
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton, C.M., Aldea, M., Washburn, B.K., Babitzke, P. and Kushner, S. (1989) New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol., 177, 4617-4622.
    • (1989) J. Bacteriol. , vol.177 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.5
  • 24
    • 0024835265 scopus 로고
    • Selection of the initiator tRNA by Escherichia coli initiation factor
    • Hartz, D., McPheeters, D.S. and Gold, L. (1989) Selection of the initiator tRNA by Escherichia coli initiation factor. Genes Dev., 3, 1899-1912.
    • (1989) Genes Dev. , vol.3 , pp. 1899-1912
    • Hartz, D.1    McPheeters, D.S.2    Gold, L.3
  • 25
    • 0026739536 scopus 로고
    • Coding from a distance: Dissection of the mRNA determinants required for the incorporation of selenocysteine into protein
    • Heider, J., Baron, C. and Böck, A. (1992) Coding from a distance: dissection of the mRNA determinants required for the incorporation of selenocysteine into protein. EMBO J., 11, 3759-3766.
    • (1992) EMBO J. , vol.11 , pp. 3759-3766
    • Heider, J.1    Baron, C.2    Böck, A.3
  • 26
    • 0030425121 scopus 로고    scopus 로고
    • Structural model for the selenocysteine-specific elongation factor SelB
    • Hilgenfeld, R., Böck, A. and Wilting, R. (1996) Structural model for the selenocysteine-specific elongation factor SelB. Biochimie, 78, 971-978.
    • (1996) Biochimie , vol.78 , pp. 971-978
    • Hilgenfeld, R.1    Böck, A.2    Wilting, R.3
  • 27
    • 0040710139 scopus 로고    scopus 로고
    • Selenocysteine inserting RNA elements modulate GTP hydrolysis of elongation factor SELB
    • Hüttenhofer, A. and Böck, A. (1998) Selenocysteine inserting RNA elements modulate GTP hydrolysis of elongation factor SELB. Biochemistry, 37, 885-890.
    • (1998) Biochemistry , vol.37 , pp. 885-890
    • Hüttenhofer, A.1    Böck, A.2
  • 29
    • 0031010402 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB
    • Klug, S.J., Hüttenhofer, A., Kromayer, M. and Famulok, M. (1997) In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB. Proc. Natl Acad. Sci. USA, 94, 6676-6681.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6676-6681
    • Klug, S.J.1    Hüttenhofer, A.2    Kromayer, M.3    Famulok, M.4
  • 30
    • 0029916386 scopus 로고    scopus 로고
    • Analysis of eukaryotic mRNA structures directing cotranslational incorporation of selenocysteine
    • Kollmus, H., Flohé, L. and McCarthy, J.E.G. (1996) Analysis of eukaryotic mRNA structures directing cotranslational incorporation of selenocysteine. Nucleic Acids Res., 24, 1195-1201.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1195-1201
    • Kollmus, H.1    Flohé, L.2    McCarthy, J.E.G.3
  • 31
    • 0030568977 scopus 로고    scopus 로고
    • Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB
    • Kromayer, M., Wilting, R., Tormay, P. and Böck, A. (1996) Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB. J. Mol. Biol., 262, 413-420.
    • (1996) J. Mol. Biol. , vol.262 , pp. 413-420
    • Kromayer, M.1    Wilting, R.2    Tormay, P.3    Böck, A.4
  • 32
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. I. DNA packing events
    • Laemmli, U.K. and Favre, M. (1973) Maturation of the head of bacteriophage T4. I. DNA packing events. J. Mol. Biol., 80, 575-599.
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 34
    • 0023787932 scopus 로고
    • pACYC184 derived cloning vectors containing the multiple cloning site and lacZα reporter gene of pUC8/9 and pUC18/19 plasmids
    • Martinez, E., Bartolomé, B. and Cruz, F.D.L. (1988) pACYC184 derived cloning vectors containing the multiple cloning site and lacZα reporter gene of pUC8/9 and pUC18/19 plasmids. Gene, 68, 159-162.
    • (1988) Gene , vol.68 , pp. 159-162
    • Martinez, E.1    Bartolomé, B.2    Cruz, F.D.L.3
  • 35
    • 0020645043 scopus 로고
    • New M13 vectors for cloning
    • Messing, J. (1983) New M13 vectors for cloning. Methods Enzymol., 101, 20-78.
    • (1983) Methods Enzymol. , vol.101 , pp. 20-78
    • Messing, J.1
  • 36
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, NY
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 37
    • 0020583709 scopus 로고
    • Effects of surrounding sequence on the suppression of nonsense codons
    • Miller, J.H. and Albertini, A.M. (1983) Effects of surrounding sequence on the suppression of nonsense codons. J. Mol. Biol., 164, 59-71.
    • (1983) J. Mol. Biol. , vol.164 , pp. 59-71
    • Miller, J.H.1    Albertini, A.M.2
  • 40
    • 0016667190 scopus 로고
    • Complications in the simplest cellular enzyme assay: Lysis of Escherichia coli for the assay of β-galactosidase
    • Putnam, S.L. and Koch, A.L. (1975) Complications in the simplest cellular enzyme assay: lysis of Escherichia coli for the assay of β-galactosidase. Anal. Biochem., 63, 350-360.
    • (1975) Anal. Biochem. , vol.63 , pp. 350-360
    • Putnam, S.L.1    Koch, A.L.2
  • 41
    • 0021164969 scopus 로고
    • Defined set of cloned termination suppressors: In vivo activity of isogenetic UAG, UAA and UGA sup tRNAs
    • Raftery, L.A., Egan, J.B., Cline, S.W. and Yarus, M. (1984) Defined set of cloned termination suppressors: in vivo activity of isogenetic UAG, UAA and UGA sup tRNAs. J. Bacteriol., 158, 849-859.
    • (1984) J. Bacteriol. , vol.158 , pp. 849-859
    • Raftery, L.A.1    Egan, J.B.2    Cline, S.W.3    Yarus, M.4
  • 42
    • 0028118546 scopus 로고
    • Recognition of the mRNA selenocysteine insertion sequences by the specialized translation factor SelB
    • Ringquist, S., Schneider, P., Gibson, T., Baron, C., Böck, A. and Gold, L. (1994) Recognition of the mRNA selenocysteine insertion sequences by the specialized translation factor SelB. Genes Dev., 8, 376-385.
    • (1994) Genes Dev. , vol.8 , pp. 376-385
    • Ringquist, S.1    Schneider, P.2    Gibson, T.3    Baron, C.4    Böck, A.5    Gold, L.6
  • 43
    • 0015903776 scopus 로고
    • Induction kinetics of the L-arabinose operon of Escherichia coli
    • Schleif, R., Hess, W., Finkelstein, S. and Ellis, D. (1973) Induction kinetics of the L-arabinose operon of Escherichia coli. J. Bacteriol., 115, 9-14.
    • (1973) J. Bacteriol. , vol.115 , pp. 9-14
    • Schleif, R.1    Hess, W.2    Finkelstein, S.3    Ellis, D.4
  • 44
    • 0021064523 scopus 로고
    • New versatile plasmid vectors for expression of hybrid proteins coded by a cloned gene fused to lacZ gene sequences encoding an enzymatically active carboxy-terminal portion of β-galactosidase
    • Shapira, S.K., Chou, J., Richaud, F.V. and Casadaban, M.J. (1983) New versatile plasmid vectors for expression of hybrid proteins coded by a cloned gene fused to lacZ gene sequences encoding an enzymatically active carboxy-terminal portion of β-galactosidase. Gene, 25, 71-82.
    • (1983) Gene , vol.25 , pp. 71-82
    • Shapira, S.K.1    Chou, J.2    Richaud, F.V.3    Casadaban, M.J.4
  • 45
    • 0016415604 scopus 로고
    • Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria
    • Shaw, W.V. (1975) Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol., 43, 737-755.
    • (1975) Methods Enzymol. , vol.43 , pp. 737-755
    • Shaw, W.V.1
  • 46
    • 0029091802 scopus 로고
    • A channeled tRNA cycle during mammalian protein synthesis
    • Stapulionis, R. and Deutscher, M.P. (1995) A channeled tRNA cycle during mammalian protein synthesis. Proc. Natl Acad. Sci. USA, 92, 7158-7161.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7158-7161
    • Stapulionis, R.1    Deutscher, M.P.2
  • 47
    • 0031015877 scopus 로고    scopus 로고
    • Barriers to heterologous expression of a selenoprotein gene in bacteria
    • Tormay, P. and Böck, A. (1997) Barriers to heterologous expression of a selenoprotein gene in bacteria. J. Bacteriol., 179, 576-582.
    • (1997) J. Bacteriol. , vol.179 , pp. 576-582
    • Tormay, P.1    Böck, A.2
  • 48
    • 0029836620 scopus 로고    scopus 로고
    • Role of stoichiometry between mRNA, translation factor SelB and selenocysteyl-tRNA in selenoprotein synthesis
    • Tormay, P., Sawers, A. and Böck, A. (1996) Role of stoichiometry between mRNA, translation factor SelB and selenocysteyl-tRNA in selenoprotein synthesis. Mol. Microbiol., 21, 1253-1259.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1253-1259
    • Tormay, P.1    Sawers, A.2    Böck, A.3
  • 49
    • 0026043778 scopus 로고
    • Direct analysis of aminoacylation levels of tRNAs in vivo
    • Varshney, U., Lee, C.-P. and RajBhandary, U.L. (1991) Direct analysis of aminoacylation levels of tRNAs in vivo. J. Biol. Chem., 266, 18018-18024.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18018-18024
    • Varshney, U.1    Lee, C.-P.2    Rajbhandary, U.L.3
  • 50
    • 0030847410 scopus 로고    scopus 로고
    • Reported translational bypass in a trpR′-lacZ′ fusion is accounted for by unusual initiation and +1 frameshifting
    • Wills, N.M., Ingram, J.A., Gesteland, R.F. and Atkins, J.F. (1997) Reported translational bypass in a trpR′-lacZ′ fusion is accounted for by unusual initiation and +1 frameshifting. J. Mol. Biol., 271, 491-498.
    • (1997) J. Mol. Biol. , vol.271 , pp. 491-498
    • Wills, N.M.1    Ingram, J.A.2    Gesteland, R.F.3    Atkins, J.F.4
  • 51
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequence of M13mp18 and pUC19 vectors. Gene, 33, 103-109.
    • (1985) Gene , vol.33 , pp. 103-109
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 52
    • 0025341614 scopus 로고
    • Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine
    • Zinoni, F., Heider, J. and Böck, A. (1990) Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine. Proc. Natl Acad. Sci. USA, 87, 4660-4664.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4660-4664
    • Zinoni, F.1    Heider, J.2    Böck, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.