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Volumn 25, Issue 7, 2000, Pages 311-316

The Adaptor hypothesis revisited

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; AMINO ACID TRANSFER RNA LIGASE; MESSENGER RNA; RIBOZYME; TRANSFER RNA;

EID: 0034234758     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01600-5     Document Type: Note
Times cited : (109)

References (46)
  • 1
    • 0040559883 scopus 로고    scopus 로고
    • Quality control mechanisms during translation
    • 1 Ibba, M. and Söll, D. (1999) Quality control mechanisms during translation. Science 286, 1893-1897
    • (1999) Science , vol.286 , pp. 1893-1897
    • Ibba, M.1    Söll, D.2
  • 2
    • 70449209123 scopus 로고
    • On protein synthesis
    • 2 Crick, F.H.C. (1958) On protein synthesis. Symp. Soc. Exp. Biol. 12, 138-163
    • (1958) Symp. Soc. Exp. Biol. , vol.12 , pp. 138-163
    • Crick, F.H.C.1
  • 3
    • 77956921819 scopus 로고
    • Aminoacyl-tRNA synthetases
    • 3 Söll, D. and Schimmel, P.R. (1974) Aminoacyl-tRNA synthetases. The Enzymes 10, 489-538
    • (1974) The Enzymes , vol.10 , pp. 489-538
    • Söll, D.1    Schimmel, P.R.2
  • 4
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • 4 Arnez, J.G. and Moras, D. (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem. Sci. 22, 211-216
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 211-216
    • Arnez, J.G.1    Moras, D.2
  • 6
    • 0014324873 scopus 로고
    • Transfer RNA as a cofactor coupling amino acid synthesis with that of protein
    • 6 Wilcox, M. and Nirenberg, M. (1968) Transfer RNA as a cofactor coupling amino acid synthesis with that of protein. Proc. Natl. Acad. Sci. U. S. A. 61, 229-236
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.61 , pp. 229-236
    • Wilcox, M.1    Nirenberg, M.2
  • 7
    • 0015354787 scopus 로고
    • Further codon assignments in an extremely halophilic bacterium using a cell-free protein-synthesizing system and a ribosomal binding assay
    • 7 White, B.N. and Bayley, S.T. (1972) Further codon assignments in an extremely halophilic bacterium using a cell-free protein-synthesizing system and a ribosomal binding assay. Can. J. Biochem. 50, 600-609
    • (1972) Can. J. Biochem. , vol.50 , pp. 600-609
    • White, B.N.1    Bayley, S.T.2
  • 8
    • 0017661126 scopus 로고
    • Yeast mitochondrial DNA specifies tRNA for 19 amino acids. Deletion mapping of the tRNA genes
    • 8 Martin, N.C. et al. (1977) Yeast mitochondrial DNA specifies tRNA for 19 amino acids. Deletion mapping of the tRNA genes. Biochemistry 16, 4672-4677
    • (1977) Biochemistry , vol.16 , pp. 4672-4677
    • Martin, N.C.1
  • 9
    • 0024285823 scopus 로고
    • Protein biosynthesis in organelles requires misaminoacylation of tRNA
    • 9 Schön, A. et al. (1988) Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature 331, 187-190
    • (1988) Nature , vol.331 , pp. 187-190
    • Schön, A.1
  • 10
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeonx, Methanococcus jannaschii
    • 10 Bult, C.J. et al. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 1058-1073
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 11
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum δH: Functional analysis and comparative genomics
    • 11 Smith, D.R. et al. (1997) Complete genome sequence of Methanobacterium thermoautotrophicum δH: functional analysis and comparative genomics. J. Bacteriol. 179, 7135-7155
    • (1997) J. Bacteriol. , vol.179 , pp. 7135-7155
    • Smith, D.R.1
  • 12
    • 0029781454 scopus 로고    scopus 로고
    • tRNA-dependent asparagine formation
    • 12 Curnow, A.W. et al. (1996) tRNA-dependent asparagine formation. Nature 382, 589-590
    • (1996) Nature , vol.382 , pp. 589-590
    • Curnow, A.W.1
  • 13
    • 0030613553 scopus 로고    scopus 로고
    • Gln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
    • Gln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation. Proc. Natl. Acad. Sci. U. S. A. 94, 11819-11826
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11819-11826
    • Curnow, A.W.1
  • 14
    • 0032573080 scopus 로고    scopus 로고
    • Gln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis
    • Gln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 95, 12838-12843
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12838-12843
    • Curnow, A.W.1
  • 16
    • 0029666265 scopus 로고    scopus 로고
    • Gln transamidation pathway among bacteria
    • Gln transamidation pathway among bacteria. J. Biol. Chem. 271, 14856-14863
    • (1996) J. Biol. Chem. , vol.271 , pp. 14856-14863
    • Gagnon, Y.1
  • 17
    • 8944231644 scopus 로고    scopus 로고
    • Asn-tRNA in Lactobacillus bulgaricus is formed by asparaginylation of tRNA and not by transamidation of Asp-tRNA
    • 17 Kim, S.I. et al. (1996) Asn-tRNA in Lactobacillus bulgaricus is formed by asparaginylation of tRNA and not by transamidation of Asp-tRNA. Nucleic Acids Res. 24, 2648-2651
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2648-2651
    • Kim, S.I.1
  • 18
    • 0032573150 scopus 로고    scopus 로고
    • Thermus thermophilus: A link in evolution of the tRNA-dependent amino acid amidation pathways
    • 18 Becker, H.D. and Kern, D. (1998) Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways. Proc. Natl. Acad. Sci. U. S. A. 95, 12832-12837
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12832-12837
    • Becker, H.D.1    Kern, D.2
  • 19
    • 0030791314 scopus 로고    scopus 로고
    • Leishmania tarentolae contains distinct cytosolic and mitochondrial glutaminyl-tRNA synthetase activities
    • 19 Nabholz, C.E. et al. (1997) Leishmania tarentolae contains distinct cytosolic and mitochondrial glutaminyl-tRNA synthetase activities. Proc. Natl. Acad. Sci. U. S. A. 94, 7903-7908
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7903-7908
    • Nabholz, C.E.1
  • 20
    • 0033280664 scopus 로고    scopus 로고
    • An attempt to pinpoint the phylogenetic introduction of glutaminyl-tRNA synthetase among bacteria
    • 20 Handy, J. and Doolittle, R.F. (1999) An attempt to pinpoint the phylogenetic introduction of glutaminyl-tRNA synthetase among bacteria. J. Mol. Evol. 49, 709-715
    • (1999) J. Mol. Evol. , vol.49 , pp. 709-715
    • Handy, J.1    Doolittle, R.F.2
  • 21
    • 0027992228 scopus 로고
    • Evolution of the Glx-tRNA synthetase family: The glutaminyl enzyme as a case of horizontal gene transfer
    • 21 Lamour, V. et al. (1994) Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc. Natl. Acad. Sci. U. S. A. 91, 8670-8674
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8670-8674
    • Lamour, V.1
  • 22
    • 0032844737 scopus 로고    scopus 로고
    • Gene descent, duplication, and horizontal transfer in the evolution of glutamyl-and glutaminyl-tRNA synthetases
    • 22 Brown, J.R. and Doolittle, W.F. (1999) Gene descent, duplication, and horizontal transfer in the evolution of glutamyl-and glutaminyl-tRNA synthetases. J. Mol. Evol. 49, 4854-4895
    • (1999) J. Mol. Evol. , vol.49 , pp. 4854-4895
    • Brown, J.R.1    Doolittle, W.F.2
  • 23
    • 0344994571 scopus 로고    scopus 로고
    • Archaeal aminoacyl-tRNA synthesis: Diversity replaces dogma
    • 23 Tumbula, D.L. et al. (1999) Archaeal aminoacyl-tRNA synthesis: diversity replaces dogma. Genetics 152, 1269-1276
    • (1999) Genetics , vol.152 , pp. 1269-1276
    • Tumbula, D.L.1
  • 24
    • 0034053846 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process
    • 24 Woese, C.R. et al. (2000) Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol. Mol. Biol. Rev. 64, 202-236
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 202-236
    • Woese, C.R.1
  • 25
    • 0017749245 scopus 로고
    • The concept of cellular evolution
    • 25 Woese, C.R. and Fox, G.E. (1977) The concept of cellular evolution J. Mol. Evol. 10, 1-6
    • (1977) J. Mol. Evol. , vol.10 , pp. 1-6
    • Woese, C.R.1    Fox, G.E.2
  • 26
    • 0033582265 scopus 로고    scopus 로고
    • Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement
    • 26 Ibba, M. et al. (1999) Substrate recognition by class I lysyl-tRNA synthetases: a molecular basis for gene displacement. Proc. Natl. Acad. Sci. U. S. A. 96, 418-423
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 418-423
    • Ibba, M.1
  • 27
    • 0034695470 scopus 로고    scopus 로고
    • One polypeptide with two aminoacyl-tRNA synthetase activities
    • 27 Stathopoulos, C. et al. (2000) One polypeptide with two aminoacyl-tRNA synthetase activities. Science 287, 479-482
    • (2000) Science , vol.287 , pp. 479-482
    • Stathopoulos, C.1
  • 28
    • 0032518606 scopus 로고    scopus 로고
    • Pro anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase
    • Pro anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase. Structure 15, 101-108
    • (1998) Structure , vol.15 , pp. 101-108
    • Cusack, S.1
  • 31
    • 0030658811 scopus 로고    scopus 로고
    • Maintaining genetic code through adaptations of tRNA synthetases to taxonomic domains
    • 31 Shiba, K. et al. (1997) Maintaining genetic code through adaptations of tRNA synthetases to taxonomic domains. Trends Biochem. Sci. 22, 453-457
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 453-457
    • Shiba, K.1
  • 32
    • 0033213625 scopus 로고    scopus 로고
    • Transfer RNA-dependent translocation of misactivated amino acids to prevent errors in protein synthesis
    • 32 Nomanbhoy, T.K. et al. (1999) Transfer RNA-dependent translocation of misactivated amino acids to prevent errors in protein synthesis. Mol. Cell 4, 519-528
    • (1999) Mol. Cell , vol.4 , pp. 519-528
    • Nomanbhoy, T.K.1
  • 33
    • 0342514827 scopus 로고    scopus 로고
    • Cysteine biosynthesis in the archaeon Methanosarcina barkeri encoded by acquired bacterial genes?
    • 33 Kitabatake, M. et al. (2000) Cysteine biosynthesis in the archaeon Methanosarcina barkeri encoded by acquired bacterial genes? J. Bacteriol. 182, 143-145
    • (2000) J. Bacteriol. , vol.182 , pp. 143-145
    • Kitabatake, M.1
  • 34
    • 0032764518 scopus 로고    scopus 로고
    • Global transposon mutagenesis and a minimal Mycoplasma genome
    • 34 Hutchison, C.A. III (1999) Global transposon mutagenesis and a minimal Mycoplasma genome. Science 286, 2165-2169
    • (1999) Science , vol.286 , pp. 2165-2169
    • Hutchison C.A. III1
  • 35
    • 0033581875 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases on the loose
    • 35 Weiner, A.M. (1999) Aminoacyl-tRNA synthetases on the loose. Curr. Biol. 18, 842-844
    • (1999) Curr. Biol. , vol.18 , pp. 842-844
    • Weiner, A.M.1
  • 36
    • 0033977761 scopus 로고    scopus 로고
    • The RNA world, the genetic code and the tRNA molecule
    • 36 Di Giulio, M. (2000) The RNA world, the genetic code and the tRNA molecule. Trends Genet. 16, 17-19
    • (2000) Trends Genet. , vol.16 , pp. 17-19
    • Di Giulio, M.1
  • 38
    • 0029009371 scopus 로고
    • Transfer RNA: From minihelix to genetic code
    • 38 Schimmel, P. and Ribas de Pouplana, L. (1995) Transfer RNA: from minihelix to genetic code. Cell 81, 983-986
    • (1995) Cell , vol.81 , pp. 983-986
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 39
    • 0003604405 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press
    • 39 Gesteland, R.F. et al. (1999) The RNA World, Cold Spring Harbor Laboratory Press
    • (1999) The RNA World
    • Gesteland, R.F.1
  • 40
    • 0028338701 scopus 로고
    • Phylogeny from function: Evidence from the molecular fossil record that tRNA originated in replication, not translation
    • 40 Maizels, N. and Weiner, A.M. (1994) Phylogeny from function: evidence from the molecular fossil record that tRNA originated in replication, not translation. Proc. Natl. Acad. Sci. U. S. A. 91, 6729-6734
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 6729-6734
    • Maizels, N.1    Weiner, A.M.2
  • 41
    • 0032530786 scopus 로고    scopus 로고
    • Genetic code origins: tRNAs older than their synthetases?
    • 41 Ribas de Pouplana, L. et al. (1998) Genetic code origins: tRNAs older than their synthetases? Proc. Natl. Acad. Sci. U. S. A. 95, 11295-11300
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11295-11300
    • Ribas De Pouplana, L.1
  • 42
    • 0033987612 scopus 로고    scopus 로고
    • Ribozyme-catalysed tRNA aminoacylation
    • 42 Lee, N. et al. (2000) Ribozyme-catalysed tRNA aminoacylation. Nat. Struct. Biol. 7, 28-33
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 28-33
    • Lee, N.1
  • 43
    • 0031081750 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis: Divergent routes to a common goal
    • 43 Ibba, M. et al. (1997) Aminoacyl-tRNA synthesis: divergent routes to a common goal. Trends Biochem. Sci. 22, 39-42
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 39-42
    • Ibba, M.1
  • 45
    • 0029591936 scopus 로고
    • Partition of aminoacyl-tRNA synthetases in two different structural classes dating back to early metabolism: Implications for the origin of the genetic code and the nature of protein sequences
    • 45 Delarue, M. (1995) Partition of aminoacyl-tRNA synthetases in two different structural classes dating back to early metabolism: implications for the origin of the genetic code and the nature of protein sequences. J. Mol. Evol. 41, 703-711
    • (1995) J. Mol. Evol. , vol.41 , pp. 703-711
    • Delarue, M.1
  • 46
    • 0028969559 scopus 로고
    • Phylogenetic analysis of the aminoacyl-tRNA synthetases
    • 46 Nagel, G.M. and Doolittle, R.F. (1995) Phylogenetic analysis of the aminoacyl-tRNA synthetases. J. Mol. Evol. 40, 487-498
    • (1995) J. Mol. Evol. , vol.40 , pp. 487-498
    • Nagel, G.M.1    Doolittle, R.F.2


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