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Volumn 18, Issue 12, 1999, Pages 3475-3483

Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus

Author keywords

RNA recognition; RNA world; RNA protein interactions; tRNA evolution; tRNA synthetase

Indexed keywords

CHAPERONE; POLYACRYLAMIDE GEL; RNA BINDING PROTEIN; TRANSFER RNA;

EID: 0033564649     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.12.3475     Document Type: Article
Times cited : (73)

References (58)
  • 2
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • 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
  • 3
    • 0029127816 scopus 로고
    • Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
    • Arnez, J.G., Harris, D.C., Mitschler, A., Rees, B., Francklyn, C.S. and Moras, D. (1995) Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO J., 14, 4143-4155.
    • (1995) EMBO J. , vol.14 , pp. 4143-4155
    • Arnez, J.G.1    Harris, D.C.2    Mitschler, A.3    Rees, B.4    Francklyn, C.S.5    Moras, D.6
  • 4
    • 0029819318 scopus 로고    scopus 로고
    • The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny
    • Baldauf, S.L., Palmer, J.D. and Doolittle, W.F. (1996) The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny. Proc. Natl Acad. Sci. USA, 93, 7749-7754.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7749-7754
    • Baldauf, S.L.1    Palmer, J.D.2    Doolittle, W.F.3
  • 5
    • 0020352528 scopus 로고
    • Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment
    • Barker, D.G., Ebel, J.P., Jakes, R. and Bruton, C.J. (1982) Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment. Eur. J. Biochem., 127, 449-457.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 449-457
    • Barker, D.G.1    Ebel, J.P.2    Jakes, R.3    Bruton, C.J.4
  • 6
    • 0028105601 scopus 로고
    • The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA (Ser)
    • Biou, V., Yaremchuk, A., Tukalo, M. and Cusack, S. (1994) The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA (Ser). Science, 263, 1404-1410.
    • (1994) Science , vol.263 , pp. 1404-1410
    • Biou, V.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 7
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F.R. et al. (1997) The complete genome sequence of Escherichia coli K-12. Science, 277, 1453-1474.
    • (1997) Science , vol.277 , pp. 1453-1474
    • Blattner, F.R.1
  • 8
    • 0029912353 scopus 로고    scopus 로고
    • Sensitivity of ribosomes of the hyperthermophilic bacterium Aquifex pyrophilus to aminoglycoside antibiotics
    • Bocchetta, M., Huber, R. and Cammarano, P. (1996) Sensitivity of ribosomes of the hyperthermophilic bacterium Aquifex pyrophilus to aminoglycoside antibiotics. J. Bacteriol., 178, 1762-1765.
    • (1996) J. Bacteriol. , vol.178 , pp. 1762-1765
    • Bocchetta, M.1    Huber, R.2    Cammarano, P.3
  • 9
    • 0028941917 scopus 로고
    • Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications
    • Brown, J.R. and Doolittle, W.F. (1995) Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications. Proc. Natl Acad. Sci. USA, 92, 2441-2445.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2441-2445
    • Brown, J.R.1    Doolittle, W.F.2
  • 10
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr., D54, 905-921.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 905-921
    • Brünger, A.T.1
  • 11
    • 0026346185 scopus 로고
    • Gel retardation
    • Carey, J. (1991) Gel Retardation. Methods Enzymol., 208, 103-117.
    • (1991) Methods Enzymol. , vol.208 , pp. 103-117
    • Carey, J.1
  • 12
    • 0027255483 scopus 로고
    • Cognition, mechanism and evolutionary relationships in aminoacyl-tRNA synthetases
    • Carter, C.W., Jr (1993) Cognition, mechanism and evolutionary relationships in aminoacyl-tRNA synthetases. Annu. Rev. Biochem., 62, 715-748.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 715-748
    • Carter C.W., Jr.1
  • 13
    • 0015243237 scopus 로고
    • Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme
    • Cassio, D. and Waller, J.P. (1971) Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme. Eur. J. Biochem., 20, 283-300.
    • (1971) Eur. J. Biochem. , vol.20 , pp. 283-300
    • Cassio, D.1    Waller, J.P.2
  • 14
    • 0027411514 scopus 로고
    • Yeast tRNA (Asp) recognition by its cognate class II aminoacyl-tRNA synthetase
    • Cavarelli, J., Rees, B., Ruff, M., Thierry, J.C. and Moras, D. (1993) Yeast tRNA (Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature, 362, 181-184.
    • (1993) Nature , vol.362 , pp. 181-184
    • Cavarelli, J.1    Rees, B.2    Ruff, M.3    Thierry, J.C.4    Moras, D.5
  • 15
    • 0027756744 scopus 로고
    • The efficiency and versatility of catalytic RNA: Implications for an RNA world
    • Cech, T.R. (1993) The efficiency and versatility of catalytic RNA: implications for an RNA world. Gene, 135, 33-36.
    • (1993) Gene , vol.135 , pp. 33-36
    • Cech, T.R.1
  • 16
    • 0031456444 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases
    • Cusack, S. (1997) Aminoacyl-tRNA synthetases. Curr. Opin. Struct. Biol., 7, 881-889.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 881-889
    • Cusack, S.1
  • 17
    • 0032568375 scopus 로고    scopus 로고
    • The complete genome of the hyperthermophilic bacterium Aquifex aeolicus
    • Deckert, G. et al. (1998) The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature, 392, 353-358.
    • (1998) Nature , vol.392 , pp. 353-358
    • Deckert, G.1
  • 18
    • 0024959463 scopus 로고
    • Aminoacylation of RNA minihelices with alanine
    • Francklyn, C. and Schimmel, P. (1989) Aminoacylation of RNA minihelices with alanine. Nature, 337, 478-481.
    • (1989) Nature , vol.337 , pp. 478-481
    • Francklyn, C.1    Schimmel, P.2
  • 19
    • 0028213965 scopus 로고
    • Efficient aminoacylation of resected RNA helices by class II aspartyl-tRNA synthetase dependent on a single nucleotide
    • Frugier, M., Florentz, C. and Giegé, R. (1994) Efficient aminoacylation of resected RNA helices by class II aspartyl-tRNA synthetase dependent on a single nucleotide. EMBO J., 13, 2219-2226.
    • (1994) EMBO J. , vol.13 , pp. 2219-2226
    • Frugier, M.1    Florentz, C.2    Giegé, R.3
  • 21
    • 36849148382 scopus 로고
    • The RNA world
    • Gilbert, W. (1986) The RNA world. Nature, 319, 618.
    • (1986) Nature , vol.319 , pp. 618
    • Gilbert, W.1
  • 22
    • 0030848935 scopus 로고    scopus 로고
    • An RNA structural determinant for tRNA recognition
    • Hamann, C.S. and Hou, Y.M. (1997) An RNA structural determinant for tRNA recognition. Biochemistry, 36, 7967-7972.
    • (1997) Biochemistry , vol.36 , pp. 7967-7972
    • Hamann, C.S.1    Hou, Y.M.2
  • 23
    • 0010418390 scopus 로고
    • Molecular replacement
    • SERC Daresbury Laboratory, Warrington, UK
    • Huber, R. (1995) Molecular replacement. In Proceedings of the Daresbury Study Weekend. SERC Daresbury Laboratory, Warrington, UK, pp. 58-61.
    • (1995) Proceedings of the Daresbury Study Weekend , pp. 58-61
    • Huber, R.1
  • 24
    • 0026781869 scopus 로고
    • Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms
    • Kao, J. et al. (1992) Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms. J. Biol. Chem., 267, 20239-20247.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20239-20247
    • Kao, J.1
  • 25
    • 0028181594 scopus 로고
    • The mauriceville plasmid of Neurospora spp. uses novel mechanisms for initiating reverse transcription in vivo
    • Kennell, J.C., Wang, H. and Lambowitz, A.M. (1994) The Mauriceville plasmid of Neurospora spp. uses novel mechanisms for initiating reverse transcription in vivo. Mol. Cell. Biol., 14, 3094-3107.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3094-3107
    • Kennell, J.C.1    Wang, H.2    Lambowitz, A.M.3
  • 26
    • 0028273032 scopus 로고
    • The multienzyme complex containing nine aminoacyl-tRNA synthetases is ubiquitous from Drosophila to mammals
    • Kerjan, P., Cerini, C., Semeriva, M. and Mirande, M. (1994) The multienzyme complex containing nine aminoacyl-tRNA synthetases is ubiquitous from Drosophila to mammals. Biochim. Biophys. Acta, 1199, 293-297.
    • (1994) Biochim. Biophys. Acta , vol.1199 , pp. 293-297
    • Kerjan, P.1    Cerini, C.2    Semeriva, M.3    Mirande, M.4
  • 28
    • 0030945598 scopus 로고    scopus 로고
    • Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine
    • Kleeman, T.A., Wei, D., Simpson, K.L. and First, E.A. (1997) Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J. Biol. Chem., 272, 14420-14425.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14420-14425
    • Kleeman, T.A.1    Wei, D.2    Simpson, K.L.3    First, E.A.4
  • 29
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding, Rowe and Horton (eds), Royal Society of Chemistry, Cambridge, UK
    • Laue, T.M., Shah, B.D., Ridgeway, T.M. and Pelletier, S.L. (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In Harding, Rowe and Horton (eds), Analytical Ultracentrifugation in Biochemistry and Polymer Science. Royal Society of Chemistry, Cambridge, UK, pp. 90-125.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 30
    • 0002630888 scopus 로고
    • The genomic tag hypotheis: Modern viruses as molecular fossils of ancient strategies for genomic replication
    • Gesteland, R.F. and Atkins, R.F. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Maizels, N. and Weiner, A.M. (1993) The genomic tag hypotheis: modern viruses as molecular fossils of ancient strategies for genomic replication. In Gesteland, R.F. and Atkins, R.F. (eds), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, p. 630.
    • (1993) The RNA World , pp. 630
    • Maizels, N.1    Weiner, A.M.2
  • 31
    • 0001163067 scopus 로고    scopus 로고
    • Small RNA oligonucleotide substrates for specific aminoacylations
    • Söll, D. and RajBhandary, U.L. (eds), ASM Press, Washington, DC
    • Martinis, S.A. and Schimmel, P. (1996) Small RNA oligonucleotide substrates for specific aminoacylations. In Söll, D. and RajBhandary, U.L. (eds), tRNA: Structure, Biosynthesis and Function. ASM Press, Washington, DC, pp. 335-349.
    • (1996) tRNA: Structure, Biosynthesis and Function , pp. 335-349
    • Martinis, S.A.1    Schimmel, P.2
  • 34
    • 0027361278 scopus 로고
    • Structural aspects and evolutionary implications of the recognition between tRNAs and aminoacyl-tRNA synthetases
    • Moras, D. (1993) Structural aspects and evolutionary implications of the recognition between tRNAs and aminoacyl-tRNA synthetases. Biochimie, 75, 651-657.
    • (1993) Biochimie , vol.75 , pp. 651-657
    • Moras, D.1
  • 36
    • 0003173754 scopus 로고
    • On the origin of the ribosome: Coevolution of subdomains of tRNA and rRNA
    • Gesteland and Atkins (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Noller, H.F. (1993) On the origin of the ribosome: coevolution of subdomains of tRNA and rRNA. In Gesteland and Atkins (eds), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 137-156.
    • (1993) The RNA World , pp. 137-156
    • Noller, H.F.1
  • 37
    • 0028266202 scopus 로고
    • Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli
    • Nureki, O., Niimi, T., Muramatsu, T., Kanno, H., Kohno, T., Florentz, C., Giegé, R. and Yokoyama, S. (1994) Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli. J. Mol. Biol., 236, 710-724.
    • (1994) J. Mol. Biol. , vol.236 , pp. 710-724
    • Nureki, O.1    Niimi, T.2    Muramatsu, T.3    Kanno, H.4    Kohno, T.5    Florentz, C.6    Giegé, R.7    Yokoyama, S.8
  • 39
    • 0022330784 scopus 로고
    • RNA catalysis and the origin of life
    • Pace, N.R. and Marsh, T.L. (1985) RNA catalysis and the origin of life. Orig. Life, 16, 97-116.
    • (1985) Orig. Life , vol.16 , pp. 97-116
    • Pace, N.R.1    Marsh, T.L.2
  • 40
    • 0002682751 scopus 로고
    • Measuring sedimentation, diffusion and molecular weights of small molecules by direct fitting of sedimentation velocity concentration profiles
    • Schuster, T.M. and Laue, T.M. (eds), Birkhauser, Boston, MA
    • Philo, J. (1994) Measuring sedimentation, diffusion and molecular weights of small molecules by direct fitting of sedimentation velocity concentration profiles. In Schuster, T.M. and Laue, T.M. (eds), Modern Analytical Ultracentrifugation. Birkhauser, Boston, MA, pp. 156-170.
    • (1994) Modern Analytical Ultracentrifugation , pp. 156-170
    • Philo, J.1
  • 41
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low-molecular-weight solutes
    • Philo, J.S. (1997) An improved function for fitting sedimentation velocity data for low-molecular-weight solutes. Biophys. J., 72, 435-444.
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.S.1
  • 43
    • 0031464187 scopus 로고    scopus 로고
    • The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine
    • Quevillon, S., Agou, F., Robinson, J.C. and Mirande, M. (1997) The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine. J. Biol. Chem., 272, 32573-32579.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32573-32579
    • Quevillon, S.1    Agou, F.2    Robinson, J.C.3    Mirande, M.4
  • 46
    • 0029890043 scopus 로고    scopus 로고
    • Variant minihelix RNAs reveal sequence-specific recognition of the helical tRNA (Ser) acceptor stem by E.coli seryl-tRNA synthetase
    • Saks, M.E. and Sampson, J.R. (1996) Variant minihelix RNAs reveal sequence-specific recognition of the helical tRNA (Ser) acceptor stem by E.coli seryl-tRNA synthetase. EMBO J., 15, 2843-2849.
    • (1996) EMBO J. , vol.15 , pp. 2843-2849
    • Saks, M.E.1    Sampson, J.R.2
  • 47
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide 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
    • Schagger, H.1    Von Jagow, G.2
  • 48
    • 0029009371 scopus 로고
    • Transfer RNA: From minihelix to genetic code
    • 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
  • 49
    • 0027436686 scopus 로고
    • An operational RNA code for amino acids and possible relationship to genetic code
    • Schimmel, P., Giegé, R., Moras, D. and Yokoyama, S. (1993) An operational RNA code for amino acids and possible relationship to genetic code. Proc. Natl Acad. Sci. USA, 90, 8763-8768.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8763-8768
    • Schimmel, P.1    Giegé, R.2    Moras, D.3    Yokoyama, S.4
  • 50
    • 0022131865 scopus 로고
    • On the origin of RNA splicing and introns
    • Sharp, P.A. (1985) On the origin of RNA splicing and introns. Cell, 42, 397-400.
    • (1985) Cell , vol.42 , pp. 397-400
    • Sharp, P.A.1
  • 52
    • 0029790980 scopus 로고    scopus 로고
    • The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl-and glutamyl-tRNA synthetases
    • Simos, G., Segref, A., Fasiolo, F., Hellmuth, K., Shevchenko, A., Mann, M. and Hurt, E.C. (1996) The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl-and glutamyl-tRNA synthetases. EMBO J., 15, 5437-5448.
    • (1996) EMBO J. , vol.15 , pp. 5437-5448
    • Simos, G.1    Segref, A.2    Fasiolo, F.3    Hellmuth, K.4    Shevchenko, A.5    Mann, M.6    Hurt, E.C.7
  • 53
    • 0031610693 scopus 로고    scopus 로고
    • A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases
    • Simos, G., Sauer, A., Fasiolo, F. and Hurt, E.C. (1998) A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol. Cell, 1, 235-242.
    • (1998) Mol. Cell , vol.1 , pp. 235-242
    • Simos, G.1    Sauer, A.2    Fasiolo, F.3    Hurt, E.C.4
  • 54
    • 0025068619 scopus 로고
    • Structural basis of tRNA discrimination as derived from the high resolution crystal structure of glutaminyl-tRNA synthetase complexed with tRNA (Gln) and ATP
    • Steitz, T.A., Rould, M.A. and Perona, J.J. (1990) Structural basis of tRNA discrimination as derived from the high resolution crystal structure of glutaminyl-tRNA synthetase complexed with tRNA (Gln) and ATP. Mol. Biol. Rep., 14, 213-214.
    • (1990) Mol. Biol. Rep. , vol.14 , pp. 213-214
    • Steitz, T.A.1    Rould, M.A.2    Perona, J.J.3
  • 55
    • 0022479943 scopus 로고
    • Identification of peptide sequences at the tRNA binding site of Escherichia coli methionyl-tRNA synthetase
    • Valenzuela, D. and Schulman, L.H. (1986) Identification of peptide sequences at the tRNA binding site of Escherichia coli methionyl-tRNA synthetase. Biochemistry, 25, 4555-4561.
    • (1986) Biochemistry , vol.25 , pp. 4555-4561
    • Valenzuela, D.1    Schulman, L.H.2
  • 56
    • 0031059865 scopus 로고    scopus 로고
    • Overview of protein crystallization methods
    • Weber, P.C. (1997) Overview of protein crystallization methods. Methods Enzymol., 276, 13-22.
    • (1997) Methods Enzymol. , vol.276 , pp. 13-22
    • Weber, P.C.1
  • 57
    • 0023449816 scopus 로고
    • tRNA-like structures tag the 3′ ends of genomic RNA molecules for replication: Implications for the origin of protein synthesis
    • Weiner, A.M. and Maizels, N. (1987) tRNA-like structures tag the 3′ ends of genomic RNA molecules for replication: implications for the origin of protein synthesis. Proc. Natl Acad. Sci. USA, 84, 7383-7387.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7383-7387
    • Weiner, A.M.1    Maizels, N.2
  • 58
    • 0032935863 scopus 로고    scopus 로고
    • The trials and travels of tRNA
    • Wolin, S.L. and Matera, A.G. (1999) The trials and travels of tRNA. Genes Dev., 13, 1-10.
    • (1999) Genes Dev. , vol.13 , pp. 1-10
    • Wolin, S.L.1    Matera, A.G.2


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