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Volumn 48, Issue 3, 1999, Pages 291-302

Novel predicted RNA-binding domains associated with the translation machinery

Author keywords

Archaeosine transglycosylase; Pseudouridine synthase; Ribosomal protein S4; RNA binding domains; Translation machinery

Indexed keywords

ADENOSINE DERIVATIVE; RIBOSOME RNA; RNA BINDING PROTEIN; RNA METHYLTRANSFERASE; SYNTHETASE; TRANSFER RNA;

EID: 0033046425     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006472     Document Type: Article
Times cited : (173)

References (56)
  • 2
    • 0029155730 scopus 로고
    • Messenger RNA recognition by fragments of ribosomal protein S4
    • Baker A, Draper D (1995) Messenger RNA recognition by fragments of ribosomal protein S4. J Biol Chem 270:22939-22945
    • (1995) J Biol Chem , vol.270 , pp. 22939-22945
    • Baker, A.1    Draper, D.2
  • 3
    • 0030772852 scopus 로고    scopus 로고
    • The yeast gene YNL292w encodes a pseudouridine synthase (Pus4) catalyzing the formation of psi55 in both mitochondrial and cytoplasmic tRNAs
    • Becker HF, Motorin Y, Planta RJ, Grosjean H (1997) The yeast gene YNL292w encodes a pseudouridine synthase (Pus4) catalyzing the formation of psi55 in both mitochondrial and cytoplasmic tRNAs. Nucleic Acids Res 25:4493-4499
    • (1997) Nucleic Acids Res , vol.25 , pp. 4493-4499
    • Becker, H.F.1    Motorin, Y.2    Planta, R.J.3    Grosjean, H.4
  • 4
    • 0028559230 scopus 로고
    • A P-loop-like motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activity
    • Bork P, Koonin EV (1994) A P-loop-like motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activity. Proteins 20:347-355
    • (1994) Proteins , vol.20 , pp. 347-355
    • Bork, P.1    Koonin, E.V.2
  • 5
    • 0024406896 scopus 로고
    • Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate
    • Brick P, Bhat TN, Blow DM (1989) Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate. J Mol Biol 208:83-98
    • (1989) J Mol Biol , vol.208 , pp. 83-98
    • Brick, P.1    Bhat, T.N.2    Blow, D.M.3
  • 7
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the SI RNA binding domain: A member of an ancient nucleic acid-binding fold
    • Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG (1997) The solution structure of the SI RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 88:235-242
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.2    Proctor, M.3    Freund, S.M.4    Murzin, A.G.5
  • 8
    • 0031587877 scopus 로고    scopus 로고
    • Ancient ciphers: Translation in Archaea
    • Dennis PP (1997) Ancient ciphers: translation in Archaea. Cell 89: 1007-1010
    • (1997) Cell , vol.89 , pp. 1007-1010
    • Dennis, P.P.1
  • 9
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • Doherty AJ, Serpell LC, Ponting CP (1996) The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res 24:2488-2497
    • (1996) Nucleic Acids Res , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 11
    • 0027191379 scopus 로고
    • Structure of the archaeal transfer RNA nucleoside G*-15 (2-amino-4,7-dihydro-4-oxo-7-beta-D-ribofuranosyl-1H-pyrrolo[2,3-d]pyrimidine-5-carboximidamide (archaeosine))
    • Gregson JM, Crain PF, Edmonds CG, Gupta R, Hashizume T, Phillipson DW, McCloskey JA (1993) Structure of the archaeal transfer RNA nucleoside G*-15 (2-amino-4,7-dihydro-4-oxo-7-beta-D-ribofuranosyl-1H-pyrrolo[2,3-d]pyrimidine-5-carboximidamide (archaeosine)). J Biol Chem 268:10076-10086
    • (1993) J Biol Chem , vol.268 , pp. 10076-10086
    • Gregson, J.M.1    Crain, P.F.2    Edmonds, C.G.3    Gupta, R.4    Hashizume, T.5    Phillipson, D.W.6    McCloskey, J.A.7
  • 12
    • 0029975948 scopus 로고    scopus 로고
    • Disordered C-terminal domain of tyrosyl transfer-RNA synthetase: Evidence for a folded state
    • Guez-Ivanier V, Bedouelle H. (1996) Disordered C-terminal domain of tyrosyl transfer-RNA synthetase: Evidence for a folded state. J Mol Biol 255:110-120
    • (1996) J Mol Biol , vol.255 , pp. 110-120
    • Guez-Ivanier, V.1    Bedouelle, H.2
  • 13
    • 0028883219 scopus 로고
    • Directed hydroxyl radical probing of 16S rRNA using Fe(II) tethered to ribosomal protein S4
    • Heilek GM, Marusak R, Meares CF, Noller HF (1995) Directed hydroxyl radical probing of 16S rRNA using Fe(II) tethered to ribosomal protein S4. Proc Natl Acad Sci USA 92:1113-1116
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1113-1116
    • Heilek, G.M.1    Marusak, R.2    Meares, C.F.3    Noller, H.F.4
  • 16
    • 0031447172 scopus 로고    scopus 로고
    • Archaeal-type lysyl-tRNA synthetase in the lyme disease spirochete Borrelia burgdorferi
    • Ibba M, Bono JL, Rosa PA, Söll D (1997) Archaeal-type lysyl-tRNA synthetase in the lyme disease spirochete Borrelia burgdorferi. Proc Natl Acad Sci USA 94:14383-14388
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14383-14388
    • Ibba, M.1    Bono, J.L.2    Rosa, P.A.3    Söll, D.4
  • 18
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan R, Clarke S (1994) Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch Biochem Biophys 310:417-427
    • (1994) Arch Biochem Biophys , vol.310 , pp. 417-427
    • Kagan, R.1    Clarke, S.2
  • 19
    • 0029070155 scopus 로고
    • The amino acid sequence of eukaryotic translation initiation factor 1 and its similarity to yeast initiation factor SUI1
    • Kasperaitis MA, Voorma HO, Thomas AA (1995) The amino acid sequence of eukaryotic translation initiation factor 1 and its similarity to yeast initiation factor SUI1. FEBS Lett 365:47-50
    • (1995) FEBS Lett , vol.365 , pp. 47-50
    • Kasperaitis, M.A.1    Voorma, H.O.2    Thomas, A.A.3
  • 20
    • 0028357246 scopus 로고
    • Prediction of an rRNA methyltransferase domain in human tumor-specific nucleolar protein P120
    • Koonin EV (1994) Prediction of an rRNA methyltransferase domain in human tumor-specific nucleolar protein P120. Nucleic Acids Res 22:2476-2478
    • (1994) Nucleic Acids Res , vol.22 , pp. 2476-2478
    • Koonin, E.V.1
  • 21
    • 0029945504 scopus 로고    scopus 로고
    • Pseudouridine synthases: Four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases
    • Koonin EV (1996) Pseudouridine synthases: Four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases. Nucleic Acids Res 24:2411-2415
    • (1996) Nucleic Acids Res , vol.24 , pp. 2411-2415
    • Koonin, E.V.1
  • 22
    • 0032499091 scopus 로고    scopus 로고
    • Re-evaluation of translation machinery evolution
    • Koonin EV, Aravind L (1998) Re-evaluation of translation machinery evolution. Curr Biol 8:R266-R269
    • (1998) Curr Biol , vol.8
    • Koonin, E.V.1    Aravind, L.2
  • 23
    • 0029559311 scopus 로고
    • Sequence similarity analysis of Escherichia coli proteins: Functional and evolutionary implications
    • Koonin EV, Tatusov RL, Rudd KE (1995) Sequence similarity analysis of Escherichia coli proteins: Functional and evolutionary implications. Proc Natl Acad Sci USA 92:11921-11925
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11921-11925
    • Koonin, E.V.1    Tatusov, R.L.2    Rudd, K.E.3
  • 24
    • 0031915895 scopus 로고    scopus 로고
    • Universally conserved translation initiation factors
    • Kyrpides N, Woese C (1998) Universally conserved translation initiation factors. Proc Natl Acad Sci USA 95:224-228
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 224-228
    • Kyrpides, N.1    Woese, C.2
  • 25
    • 0030296854 scopus 로고    scopus 로고
    • KOW: A novel motif linking a bacterial transcription factor with ribosomal proteins
    • Kyrpides NC, Woese CR, Ouzounis CA (1996) KOW: A novel motif linking a bacterial transcription factor with ribosomal proteins. Trends Biochem Sci 21:425-426
    • (1996) Trends Biochem Sci , vol.21 , pp. 425-426
    • Kyrpides, N.C.1    Woese, C.R.2    Ouzounis, C.A.3
  • 26
    • 0028988343 scopus 로고
    • Pseudouridine and O2′-methylated nucleosides. Significance of their selective occurrence in rRNA domains that function in ribosome-catalyzed synthesis of the peptide bonds in proteins
    • Lane BG, Ofengand J, Gray MW (1995) Pseudouridine and O2′-methylated nucleosides. Significance of their selective occurrence in rRNA domains that function in ribosome-catalyzed synthesis of the peptide bonds in proteins. Biochimie 77:7-15
    • (1995) Biochimie , vol.77 , pp. 7-15
    • Lane, B.G.1    Ofengand, J.2    Gray, M.W.3
  • 28
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin A (1993) OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences. EMBO J 12:861-867
    • (1993) EMBO J , vol.12 , pp. 861-867
    • Murzin, A.1
  • 29
    • 0030002818 scopus 로고    scopus 로고
    • SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae
    • Naranda T, MacMillan E, Donahue T, Hershey J (1996) SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol Cell Biol 16:2307-2313
    • (1996) Mol Cell Biol , vol.16 , pp. 2307-2313
    • Naranda, T.1    MacMillan, E.2    Donahue, T.3    Hershey, J.4
  • 30
    • 0029056474 scopus 로고
    • Evolutionary origins of apoB mRNA editing: Catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site
    • Navaratnam N, Bhattacharya S, Fujino T, Patel D, Jarmuz AL, Scott J (1995) Evolutionary origins of apoB mRNA editing: Catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site. Cell 81:187-195
    • (1995) Cell , vol.81 , pp. 187-195
    • Navaratnam, N.1    Bhattacharya, S.2    Fujino, T.3    Patel, D.4    Jarmuz, A.L.5    Scott, J.6
  • 31
    • 0029144601 scopus 로고
    • Gibbs motif sampling: Detection of bacterial outer membrane protein repeats
    • Neuwald AF, Liu JS, Lawrence CE (1995) Gibbs motif sampling: Detection of bacterial outer membrane protein repeats. Protein Sci 4:1618-1632
    • (1995) Protein Sci , vol.4 , pp. 1618-1632
    • Neuwald, A.F.1    Liu, J.S.2    Lawrence, C.E.3
  • 33
    • 0030059640 scopus 로고    scopus 로고
    • Transcription of Bacillus subtilis degR is sigma D dependent and suppressed by multicopy proB through sigma D
    • Ogura M, Tanaka T (1996) Transcription of Bacillus subtilis degR is sigma D dependent and suppressed by multicopy proB through sigma D. J Bacteriol 178:216-222
    • (1996) J Bacteriol , vol.178 , pp. 216-222
    • Ogura, M.1    Tanaka, T.2
  • 34
    • 0029991713 scopus 로고    scopus 로고
    • Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange
    • Romier C, Reuter K, Suck D, Ficner R (1996) Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange. EMBO J 15:2850-2857
    • (1996) EMBO J , vol.15 , pp. 2850-2857
    • Romier, C.1    Reuter, K.2    Suck, D.3    Ficner, R.4
  • 35
    • 0030832831 scopus 로고    scopus 로고
    • Slight sequence variations of a common fold explain the substrate specificities of tRNA-guanine transglycosylases from the three kingdoms
    • Romier C, Meyer JE, Suck D (1997) Slight sequence variations of a common fold explain the substrate specificities of tRNA-guanine transglycosylases from the three kingdoms. FEBS Lett 416:93-98
    • (1997) FEBS Lett , vol.416 , pp. 93-98
    • Romier, C.1    Meyer, J.E.2    Suck, D.3
  • 36
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 37
    • 0031577260 scopus 로고    scopus 로고
    • Protein fold recognition by prediction-based threading
    • Rost B, Schneider R, Sander C (1997) Protein fold recognition by prediction-based threading. J Mol Biol 270:471-480
    • (1997) J Mol Biol , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 38
    • 0028670846 scopus 로고
    • N6-Adenosine methylation in mRNA: Substrate specificity and enzyme complexity
    • Rottman FM, Bokar JA, Narayan P, Shambaugh ME, Ludwiczak R (1994) N6-Adenosine methylation in mRNA: substrate specificity and enzyme complexity. Biochimie 76:1109-1114
    • (1994) Biochimie , vol.76 , pp. 1109-1114
    • Rottman, F.M.1    Bokar, J.A.2    Narayan, P.3    Shambaugh, M.E.4    Ludwiczak, R.5
  • 40
    • 0026100921 scopus 로고
    • A workbench for multiple alignment construction and analysis
    • Schuler GD, Altschul SF, Lipman DJ (1991) A workbench for multiple alignment construction and analysis. Proteins 9:180-190
    • (1991) Proteins , vol.9 , pp. 180-190
    • Schuler, G.D.1    Altschul, S.F.2    Lipman, D.J.3
  • 41
    • 0028130514 scopus 로고
    • Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating complex requiring GTP for activity
    • Schwedock JS, Liu C, Leyh TS, Long SR (1994) Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating complex requiring GTP for activity. J Bacteriol 176:7055-7064
    • (1994) J Bacteriol , vol.176 , pp. 7055-7064
    • Schwedock, J.S.1    Liu, C.2    Leyh, T.S.3    Long, S.R.4
  • 42
    • 0028907506 scopus 로고
    • Multiple RNA binding domains (RBDs) just don't add up
    • Shamoo Y, Abdul-Manan N, Williams (1995) Multiple RNA binding domains (RBDs) just don't add up. Nucleic Acids Res 23:725-728
    • (1995) Nucleic Acids Res , vol.23 , pp. 725-728
    • Shamoo, Y.1    Abdul-Manan, N.2
  • 43
    • 0030271857 scopus 로고    scopus 로고
    • Base-modification mRNA editing through deamination - The good, the bad and the unregulated
    • Smith HC, Sowden MP (1996) Base-modification mRNA editing through deamination - The good, the bad and the unregulated. Trends Genet 12:418-424
    • (1996) Trends Genet , vol.12 , pp. 418-424
    • Smith, H.C.1    Sowden, M.P.2
  • 45
    • 0024973814 scopus 로고
    • Unusual mRNA pseudoknot structure is recognized by a protein translational represser
    • Tang C, Draper D. (1989) Unusual mRNA pseudoknot structure is recognized by a protein translational represser. Cell 57:531-536
    • (1989) Cell , vol.57 , pp. 531-536
    • Tang, C.1    Draper, D.2
  • 46
    • 0028091659 scopus 로고
    • Detection of conserved segments in proteins: Iterative scanning of sequence databases with alignment blocks
    • Tatusov RL, Altschul SF, Koonin EV (1994) Detection of conserved segments in proteins: iterative scanning of sequence databases with alignment blocks. Proc Natl Acad Sci USA 91:12091-12095
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12091-12095
    • Tatusov, R.L.1    Altschul, S.F.2    Koonin, E.V.3
  • 47
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • Tatusov RL, Koonin EV, Lipman DJ (1997) A genomic perspective on protein families. Science 278:631-637
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 49
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DC, Gibson TJ (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.C.2    Gibson, T.J.3
  • 50
    • 0030963268 scopus 로고    scopus 로고
    • Function and synthesis of small nucleolar RNAs
    • Tollervey D, Kiss T (1997) Function and synthesis of small nucleolar RNAs. Curr Opin Cell Biol 9:337-342
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 337-342
    • Tollervey, D.1    Kiss, T.2
  • 51
    • 0030990061 scopus 로고    scopus 로고
    • Sequence analysis of a 33.2 kb segment from the left arm of yeast chromosome XV reveals eight known genes and ten new open reading frames including homologues of ABC transporters, inositol phosphatases and human expressed sequence tags
    • Tzermia M, Katsoulou C, Alexandraki D (1997) Sequence analysis of a 33.2 kb segment from the left arm of yeast chromosome XV reveals eight known genes and ten new open reading frames including homologues of ABC transporters, inositol phosphatases and human expressed sequence tags. Yeast 13:583-589
    • (1997) Yeast , vol.13 , pp. 583-589
    • Tzermia, M.1    Katsoulou, C.2    Alexandraki, D.3
  • 52
    • 0030792095 scopus 로고    scopus 로고
    • Biosynthesis of archaeosine, a novel derivative of 7-deazaguanosine specific to archaeal tRNA, proceeds via a pathway involving base replacement on the tRNA polynucleotide chain
    • Watanabe M, Matsuo M, Tanaka S, Akimoto H, Asahi S, Nishimura S, Katze JR, Hashizume T, Grain PF, McCloskey JA, Okada N (1997) Biosynthesis of archaeosine, a novel derivative of 7-deazaguanosine specific to archaeal tRNA, proceeds via a pathway involving base replacement on the tRNA polynucleotide chain. J Biol Chem 272:20146-20151
    • (1997) J Biol Chem , vol.272 , pp. 20146-20151
    • Watanabe, M.1    Matsuo, M.2    Tanaka, S.3    Akimoto, H.4    Asahi, S.5    Nishimura, S.6    Katze, J.R.7    Hashizume, T.8    Grain, P.F.9    McCloskey, J.A.10    Okada, N.11
  • 53
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wootton JC, Federhen S (1996) Analysis of compositionally biased regions in sequence databases. Methods Enzymol 266:554-573
    • (1996) Methods Enzymol , vol.266 , pp. 554-573
    • Wootton, J.C.1    Federhen, S.2
  • 54
    • 0029017451 scopus 로고
    • Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli
    • Wrzesinski J, Bakin A, Nurse K, Lane BG, Ofengand J (1995a) Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli. Biochemistry 34:8904-8913
    • (1995) Biochemistry , vol.34 , pp. 8904-8913
    • Wrzesinski, J.1    Bakin, A.2    Nurse, K.3    Lane, B.G.4    Ofengand, J.5
  • 55
    • 0029313081 scopus 로고
    • A dual-specificity pseudouridine synthase: An Escherichia coli synthase purified and cloned on the basis of its specificity for psi 746 in 23S RNA is also specific for psi32 in tRNA(phe)
    • Wrzesinski J, Nurse K, Bakin A, Lane BG, Ofengand J (1995b) A dual-specificity pseudouridine synthase: An Escherichia coli synthase purified and cloned on the basis of its specificity for psi 746 in 23S RNA is also specific for psi32 in tRNA(phe). RNA 1:437-448
    • (1995) RNA , vol.1 , pp. 437-448
    • Wrzesinski, J.1    Nurse, K.2    Bakin, A.3    Lane, B.G.4    Ofengand, J.5
  • 56
    • 0026609868 scopus 로고
    • The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon
    • Yoon H, Donahue T (1992) The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon. Mol Cell Biol 12:248-260
    • (1992) Mol Cell Biol , vol.12 , pp. 248-260
    • Yoon, H.1    Donahue, T.2


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