메뉴 건너뛰기




Volumn 108, Issue 52, 2011, Pages 21040-21045

An inhibitory C-terminal region dictates the specificity of A-adding enzymes

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDYLTRANSFERASE; TRANSFER RIBONUCLEIC ACID NUCLEOTIDYLTRANSFERASE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84855478202     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1116117108     Document Type: Article
Times cited : (19)

References (34)
  • 1
    • 0031804156 scopus 로고    scopus 로고
    • Compilation of tRNA sequences and sequences of tRNA genes
    • DOI 10.1093/nar/26.1.148
    • Sprinzl M, Horn C, Brown M, Ioudovitch A, Steinberg S (1998) Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res 26:148-153. (Pubitemid 28295271)
    • (1998) Nucleic Acids Research , vol.26 , Issue.1 , pp. 148-153
    • Sprinzl, M.1    Horn, C.2    Brown, M.3    Loudovltch, A.4    Steinberg, S.5
  • 2
    • 0029903451 scopus 로고    scopus 로고
    • CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: Characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae
    • Yue D, Maizels N, Weiner AM (1996) CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: Characterization of the CCA-adding enzyme from the Archaeal hyperthermophile Sulfolobus shibatae. RNA 2:895-908. (Pubitemid 26374200)
    • (1996) RNA , vol.2 , Issue.9 , pp. 895-908
    • Yue, D.1    Maizels, N.2    Weiner, A.M.3
  • 3
    • 77952313262 scopus 로고    scopus 로고
    • TRNA nucleotidyltransferases: Ancient catalysts with an unusual mechanism of polymerization
    • Betat H, Rammelt C, Mörl M (2010) tRNA nucleotidyltransferases: Ancient catalysts with an unusual mechanism of polymerization. Cell Mol Life Sci 67:1447-1463.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 1447-1463
    • Betat, H.1    Rammelt, C.2    Mörl, M.3
  • 4
    • 71549135205 scopus 로고    scopus 로고
    • TRNA-nucleotidyltransferases: Highly unusual RNA polymerases with vital functions
    • Vörtler S, Mörl M (2010) tRNA-nucleotidyltransferases: Highly unusual RNA polymerases with vital functions. FEBS Lett 584:297-302.
    • (2010) FEBS Lett , vol.584 , pp. 297-302
    • Vörtler, S.1    Mörl, M.2
  • 5
    • 0345171487 scopus 로고    scopus 로고
    • Crystal structures of an archaeal class I CCA-adding enzyme and its nucleotide complexes
    • DOI 10.1016/S1097-2765(03)00440-4
    • Xiong Y, Li F, Wang J, Weiner AM, Steitz TA (2003) Crystal structures of an Archaeal class I CCA-adding enzyme and its nucleotide complexes. Mol Cell Biochem 12:1165-1172. (Pubitemid 37492930)
    • (2003) Molecular Cell , vol.12 , Issue.5 , pp. 1165-1172
    • Xiong, Y.1    Li, F.2    Wang, J.3    Weiner, A.M.4    Steitz, T.A.5
  • 7
    • 3943089138 scopus 로고    scopus 로고
    • Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template
    • DOI 10.1038/nature02711
    • Xiong Y, Steitz TA (2004) Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template. Nature 430:640-645. (Pubitemid 39061672)
    • (2004) Nature , vol.430 , Issue.7000 , pp. 640-645
    • Xiong, Y.1    Steitz, T.A.2
  • 8
    • 47949120771 scopus 로고    scopus 로고
    • Molecular basis for maintenance of fidelity during the CCA-adding reaction by a CCA-adding enzyme
    • Toh Y, et al. (2008) Molecular basis for maintenance of fidelity during the CCA-adding reaction by a CCA-adding enzyme. EMBO J 27:1944-1952.
    • (2008) EMBO J , vol.27 , pp. 1944-1952
    • Toh, Y.1
  • 9
    • 78149385338 scopus 로고    scopus 로고
    • How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA
    • Pan B, Xiong Y, Steitz TA (2010) How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA. Science 330:937-940.
    • (2010) Science , vol.330 , pp. 937-940
    • Pan, B.1    Xiong, Y.2    Steitz, T.A.3
  • 10
    • 0037074014 scopus 로고    scopus 로고
    • Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP
    • DOI 10.1016/S0092-8674(02)01115-7
    • Li F, et al. (2002) Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP. Cell 111:815-824. (Pubitemid 36106403)
    • (2002) Cell , vol.111 , Issue.6 , pp. 815-824
    • Li, F.1    Xiong, Y.2    Wang, J.3    Cho, H.D.4    Tomita, K.5    Weiner, A.M.6    Steitz, T.A.7
  • 11
    • 24344434584 scopus 로고    scopus 로고
    • A phylogeny of bacterial RNA nucleotidyltransferases: Bacillus halodurans contains two tRNA nucleotidyltransferases
    • DOI 10.1128/JB.187.17.5927-5936.2005
    • Bralley P, Chang SA, Jones GH (2005) A phylogeny of bacterial RNA nucleotidyltransferases: Bacillus halodurans contains two tRNA nucleotidyltransferases. J Bacteriol 187:5927-5936. (Pubitemid 41262790)
    • (2005) Journal of Bacteriology , vol.187 , Issue.17 , pp. 5927-5936
    • Bralley, P.1    Chang, S.A.2    Jones, G.H.3
  • 12
    • 58149492425 scopus 로고    scopus 로고
    • Geobacter sulfurreducens contains separate C-and A-adding tRNA nucleotidyltransferases and a poly(A) polymerase
    • Bralley P, Cozad M, Jones GH (2009) Geobacter sulfurreducens contains separate C-and A-adding tRNA nucleotidyltransferases and a poly(A) polymerase. J Bacteriol 191:109-114.
    • (2009) J Bacteriol , vol.191 , pp. 109-114
    • Bralley, P.1    Cozad, M.2    Jones, G.H.3
  • 14
    • 0035834385 scopus 로고    scopus 로고
    • Collaboration between CC- and A-adding enzymes to build and repair the 3′-terminal CCA of tRNA in Aquifex aeolicus
    • DOI 10.1126/science.1063816
    • Tomita K, Weiner AM (2001) Collaboration between CC- and A-adding enzymes to build and repair the 3′-terminal CCA of tRNA in Aquifex aeolicus. Science 294:1334-1336. (Pubitemid 33063098)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1334-1336
    • Tomita, K.1    Welner, A.M.2
  • 15
    • 0037073727 scopus 로고    scopus 로고
    • Closely related CC- and A-adding enzymes collaborate to construct and repair the 3′-terminal CCA of tRNA in Synechocystis sp. and Deinococcus radiodurans
    • DOI 10.1074/jbc.M207527200
    • Tomita K, Weiner AM (2002) Closely related CC- and A-adding enzymes collaborate to construct and repair the 3′-terminal CCA of tRNA in Synechocystis species and Deinococcus radiodurans. J Biol Chem 277:48192-48198. (Pubitemid 35470769)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48192-48198
    • Tomita, K.1    Weiner, A.M.2
  • 16
    • 52649157111 scopus 로고    scopus 로고
    • A comparative analysis of two conserved motifs in bacterial poly(A) polymerase and CCA-adding enzyme
    • Just A, et al. (2008) A comparative analysis of two conserved motifs in bacterial poly(A) polymerase and CCA-adding enzyme. Nucleic Acids Res 36:5212-5220.
    • (2008) Nucleic Acids Res , vol.36 , pp. 5212-5220
    • Just, A.1
  • 17
    • 77955233990 scopus 로고    scopus 로고
    • Unusual evolution of a catalytic core element in CCA-adding enzymes
    • Hoffmeier A, et al. (2010) Unusual evolution of a catalytic core element in CCA-adding enzymes. Nucleic Acids Res 38:4436-4447.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4436-4447
    • Hoffmeier, A.1
  • 18
    • 35548959608 scopus 로고    scopus 로고
    • RNA-specific ribonucleotidyl transferases
    • DOI 10.1261/rna.652807
    • Martin G, Keller W (2007) RNA-specific ribonucleotidyl transferases. RNA 13:1834-1849. (Pubitemid 350005209)
    • (2007) RNA , vol.13 , Issue.11 , pp. 1834-1849
    • Martin, G.1    Keller, W.2
  • 19
    • 4143073655 scopus 로고    scopus 로고
    • Exchange of regions between bacterial poly(A) polymerase and the CCA-adding enzyme generates altered specificities
    • DOI 10.1016/j.molcel.2004.06.026, PII S1097276504003740
    • Betat H, Rammelt C, Martin G, Mörl M (2004) Exchange of regions between bacterial poly(A) polymerase and CCA adding enzyme generates altered specificities. Molecular cell 15:389-398. (Pubitemid 39092755)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 389-398
    • Betat, H.1    Rammelt, C.2    Martin, G.3    Morl, M.4
  • 20
    • 0032970686 scopus 로고    scopus 로고
    • Poly(A) polymerase I of Escherichia coli: Characterization of the catalytic domain, an RNA binding site and regions for the interaction with proteins involved in mRNA degradation
    • DOI 10.1046/j.1365-2958.1999.01394.x
    • Raynal LC, Carpousis AJ (1999) Poly(A) polymerase I of Escherichia coli: Characterization of the catalytic domain, an RNA binding site and regions for the interaction with proteins involved in mRNA degradation. Mol Microbiol 32:765-775. (Pubitemid 29241517)
    • (1999) Molecular Microbiology , vol.32 , Issue.4 , pp. 765-775
    • Raynal, L.C.1    Carpousis, A.J.2
  • 22
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292:195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 23
    • 0032101196 scopus 로고    scopus 로고
    • CCA addition by tRNA nucleotidyltransferase: Polymerization without translocation?
    • DOI 10.1093/emboj/17.11.3197
    • Shi PY, Maizels N, Weiner AM (1998) CCA addition by tRNA nucleotidyltransferase: Polymerization without translocation? EMBO J 17:3197-3206. (Pubitemid 28254391)
    • (1998) EMBO Journal , vol.17 , Issue.11 , pp. 3197-3206
    • Shi, P.-Y.1    Maizels, N.2    Weiner, A.M.3
  • 24
    • 2442665253 scopus 로고    scopus 로고
    • Sequence motifs that distinguish ATP(CTP):tRNA nucleotidyl transferases from eubacterial poly(A) polymerases
    • DOI 10.1261/rna.5242304
    • Martin G, Keller W (2004) Sequence motifs that distinguish ATP(CTP): tRNA nucleotidyl transferases from eubacterial poly(A) polymerases. RNA 10:899-906. (Pubitemid 38669762)
    • (2004) RNA , vol.10 , Issue.6 , pp. 899-906
    • Martin, G.1    Keller, W.2
  • 26
    • 70350786924 scopus 로고    scopus 로고
    • Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme
    • Toh Y, et al. (2009) Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme. EMBO J 28:3353-3365.
    • (2009) EMBO J , vol.28 , pp. 3353-3365
    • Toh, Y.1
  • 27
    • 42649116726 scopus 로고    scopus 로고
    • A comparative analysis of CCA-adding enzymes from human and E. coli: Differences in CCA addition and tRNA 3′-end repair
    • Lizano E, Scheibe M, Rammelt C, Betat H, Mörl M (2008) A comparative analysis of CCA-adding enzymes from human and E. coli: Differences in CCA addition and tRNA 3′-end repair. Biochimie 90:762-772.
    • (2008) Biochimie , vol.90 , pp. 762-772
    • Lizano, E.1    Scheibe, M.2    Rammelt, C.3    Betat, H.4    Mörl, M.5
  • 28
    • 33846573777 scopus 로고    scopus 로고
    • A Splice Variant of the Human CCA-adding Enzyme with Modified Activity
    • DOI 10.1016/j.jmb.2006.12.016, PII S0022283606016755
    • Lizano E, Schuster J, Müller M, Kelso J, Mörl M (2007) A splice variant of the human CCA-adding enzyme with modified activity. J Mol Biol 366:1258-1265. (Pubitemid 46186393)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.4 , pp. 1258-1265
    • Lizano, E.1    Schuster, J.2    Muller, M.3    Kelso, J.4    Morl, M.5
  • 29
    • 84889268370 scopus 로고    scopus 로고
    • Production of RNAs with homogeneous 5′ and 3′ ends
    • eds RK Hartmann, A Bindereif, A Schön, and E Westhof (Wiley-VCH, Weinheim, Germany)
    • Mörl M, Lizano E, Willkomm DK, Hartmann RK (2005) Production of RNAs with homogeneous 5′ and 3′ ends. Handbook of RNA Biochemistry, eds RK Hartmann, A Bindereif, A Schön, and E Westhof (Wiley-VCH, Weinheim, Germany), Vol 1, pp 22-35.
    • (2005) Handbook of RNA Biochemistry , vol.1 , pp. 22-35
    • Mörl, M.1    Lizano, E.2    Willkomm, D.K.3    Hartmann, R.K.4
  • 30
    • 1542365201 scopus 로고    scopus 로고
    • A universal method to produce in vitro transcripts with homogeneous 3′ ends
    • Schürer H, Lang K, Schuster J, Mörl M (2002) A universal method to produce in vitro transcripts with homogeneous 3′ ends. Nucleic Acids Res 30:e56.
    • (2002) Nucleic Acids Res , vol.30
    • Schürer, H.1    Lang, K.2    Schuster, J.3    Mörl, M.4
  • 32
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X
    • Version 2
    • Larkin MA, et al. (2007) Clustal W and Clustal X, Version 2. Bioinformatics, pp:2947-2948.
    • (2007) Bioinformatics , pp. 2947-2948
    • Larkin, M.A.1
  • 33
    • 0003437299 scopus 로고    scopus 로고
    • Version 3.6. (Department of Genome Sciences, University of Washington, Seattle), Distributed by the author
    • Felsenstein J (2005) PHYLIP (Phylogeny Inference Package), Version 3.6. (Department of Genome Sciences, University of Washington, Seattle), Distributed by the author.
    • (2005) PHYLIP (Phylogeny Inference Package)
    • Felsenstein, J.1
  • 34
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24:1596-1599. (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.