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Volumn 399, Issue 3, 2010, Pages 464-475

Structure of the mitochondrial editosome-like complex associated TUTase 1 reveals divergent mechanisms of UTP selection and domain organization

Author keywords

Mitochondria; RNA editing; Trypanosoma; TUTase

Indexed keywords

ENZYME; MESSENGER RNA; NUCLEOSIDE TRIPHOSPHATE; TERMINAL URIDYLYL TRANSFERASE; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE;

EID: 77954760175     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.04.021     Document Type: Article
Times cited : (23)

References (42)
  • 1
    • 41549094891 scopus 로고    scopus 로고
    • Terminal RNA uridylyltransferases of trypanosomes
    • Aphasizhev R., Aphasizheva I. Terminal RNA uridylyltransferases of trypanosomes. Biochim. Biophys. Acta 2008, 1779:270-280.
    • (2008) Biochim. Biophys. Acta , vol.1779 , pp. 270-280
    • Aphasizhev, R.1    Aphasizheva, I.2
  • 2
    • 58749099417 scopus 로고    scopus 로고
    • Identification and characterization of nuclear non-canonical poly(A) polymerases from Trypanosoma brucei
    • Etheridge R.D., Clemens D.M., Aphasizhev R. Identification and characterization of nuclear non-canonical poly(A) polymerases from Trypanosoma brucei. Mol. Biochem. Parasitol. 2009, 164:66-73.
    • (2009) Mol. Biochem. Parasitol. , vol.164 , pp. 66-73
    • Etheridge, R.D.1    Clemens, D.M.2    Aphasizhev, R.3
  • 3
    • 44649128170 scopus 로고    scopus 로고
    • 3' Adenylation determines mRNA abundance and monitors completion of RNA editing in T. brucei mitochondria
    • Etheridge R.D., Aphasizheva I., Gershon P.D., Aphasizhev R. 3' Adenylation determines mRNA abundance and monitors completion of RNA editing in T. brucei mitochondria. EMBO J. 2008, 27:1596-1608.
    • (2008) EMBO J. , vol.27 , pp. 1596-1608
    • Etheridge, R.D.1    Aphasizheva, I.2    Gershon, P.D.3    Aphasizhev, R.4
  • 4
    • 34447262522 scopus 로고    scopus 로고
    • Targeted depletion of a mitochondrial nucleotidyltransferase suggests the presence of multiple enzymes that polymerize mRNA 3' tails in Trypanosoma brucei mitochondria
    • Kao C.Y., Read L.K. Targeted depletion of a mitochondrial nucleotidyltransferase suggests the presence of multiple enzymes that polymerize mRNA 3' tails in Trypanosoma brucei mitochondria. Mol. Biochem. Parasitol. 2007, 154:158-169.
    • (2007) Mol. Biochem. Parasitol. , vol.154 , pp. 158-169
    • Kao, C.Y.1    Read, L.K.2
  • 5
    • 4143136579 scopus 로고    scopus 로고
    • Multiple terminal uridylyltransferases of trypanosomes
    • Aphasizhev R., Aphasizheva I., Simpson L. Multiple terminal uridylyltransferases of trypanosomes. FEBS Lett. 2004, 572:15-18.
    • (2004) FEBS Lett. , vol.572 , pp. 15-18
    • Aphasizhev, R.1    Aphasizheva, I.2    Simpson, L.3
  • 7
    • 0037040412 scopus 로고    scopus 로고
    • Trypanosome mitochondrial 3' terminal uridylyl transferase (TUTase): the key enzyme in U-insertion/deletion RNA editing
    • Aphasizhev R., Sbicego S., Peris M., Jang S.H., Aphasizheva I., Simpson A.M., et al. Trypanosome mitochondrial 3' terminal uridylyl transferase (TUTase): the key enzyme in U-insertion/deletion RNA editing. Cell 2002, 108:637-648.
    • (2002) Cell , vol.108 , pp. 637-648
    • Aphasizhev, R.1    Sbicego, S.2    Peris, M.3    Jang, S.H.4    Aphasizheva, I.5    Simpson, A.M.6
  • 8
    • 0037450771 scopus 로고    scopus 로고
    • Isolation of a U-insertion/deletion editing complex from Leishmania tarentolae mitochondria
    • Aphasizhev R., Aphasizheva I., Nelson R.E., Gao G., Simpson A.M., Kang X., et al. Isolation of a U-insertion/deletion editing complex from Leishmania tarentolae mitochondria. EMBO J. 2003, 22:913-924.
    • (2003) EMBO J. , vol.22 , pp. 913-924
    • Aphasizhev, R.1    Aphasizheva, I.2    Nelson, R.E.3    Gao, G.4    Simpson, A.M.5    Kang, X.6
  • 10
    • 77749325035 scopus 로고    scopus 로고
    • RET1-catalyzed uridylylation shapes the mitochondrial transcriptome in Trypanosoma brucei
    • Aphasizheva I., Aphasizhev R. RET1-catalyzed uridylylation shapes the mitochondrial transcriptome in Trypanosoma brucei. Mol. Cell. Biol. 2010, 30:1555-1567.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1555-1567
    • Aphasizheva, I.1    Aphasizhev, R.2
  • 11
    • 72649096964 scopus 로고    scopus 로고
    • Guide to the nomenclature of kinetoplastid RNA editing: a proposal
    • Simpson L., Aphasizhev R., Lukes J., Cruz-Reyes J. Guide to the nomenclature of kinetoplastid RNA editing: a proposal. Protist 2010, 161:2-6.
    • (2010) Protist , vol.161 , pp. 2-6
    • Simpson, L.1    Aphasizhev, R.2    Lukes, J.3    Cruz-Reyes, J.4
  • 13
    • 0038433297 scopus 로고    scopus 로고
    • TbMP57 is a 3' terminal uridylyl transferase (TUTase) of the Trypanosoma brucei editosome
    • Ernst N.L., Panicucci B., Igo R.P., Panigrahi A.K., Salavati R., Stuart K. TbMP57 is a 3' terminal uridylyl transferase (TUTase) of the Trypanosoma brucei editosome. Mol. Cell 2003, 11:1525-1536.
    • (2003) Mol. Cell , vol.11 , pp. 1525-1536
    • Ernst, N.L.1    Panicucci, B.2    Igo, R.P.3    Panigrahi, A.K.4    Salavati, R.5    Stuart, K.6
  • 14
    • 28644431836 scopus 로고    scopus 로고
    • Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei
    • Deng J., Ernst N.L., Turley S., Stuart K.D., Hol W.G. Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. EMBO J. 2005, 24:4007-4017.
    • (2005) EMBO J. , vol.24 , pp. 4007-4017
    • Deng, J.1    Ernst, N.L.2    Turley, S.3    Stuart, K.D.4    Hol, W.G.5
  • 15
    • 35548937853 scopus 로고    scopus 로고
    • Dual role of the RNA substrate in selectivity and catalysis by terminal uridylyl transferases
    • Stagno J., Aphasizheva I., Aphasizhev R., Luecke H. Dual role of the RNA substrate in selectivity and catalysis by terminal uridylyl transferases. Proc. Natl Acad. Sci. USA 2007, 104:14634-14639.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 14634-14639
    • Stagno, J.1    Aphasizheva, I.2    Aphasizhev, R.3    Luecke, H.4
  • 16
    • 2642581697 scopus 로고    scopus 로고
    • RNA-editing terminal uridylyl transferase 1: identification of functional domains by mutational analysis
    • Aphasizheva I., Aphasizhev R., Simpson L. RNA-editing terminal uridylyl transferase 1: identification of functional domains by mutational analysis. J. Biol. Chem. 2004, 279:24123-24130.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24123-24130
    • Aphasizheva, I.1    Aphasizhev, R.2    Simpson, L.3
  • 17
    • 77953723113 scopus 로고    scopus 로고
    • Mechanism of RNA editing in trypanosome mitochondria: the bimodal U-insertion activity of the core complex. J. Mol. Biol. 2010 Apr 1. [Epub ahead of print].
    • Ringpis, G. E., Aphasizheva, I., Wang, X., Huang, L., Hatfield, G. W. & Aphasizhev, R. (2010). Mechanism of RNA editing in trypanosome mitochondria: the bimodal U-insertion activity of the core complex. J. Mol. Biol. 2010 Apr 1. [Epub ahead of print].
    • (2010)
    • Ringpis, G.E.1    Aphasizheva, I.2    Wang, X.3    Huang, L.4    Hatfield, G.W.5    Aphasizhev, R.6
  • 18
    • 67649342891 scopus 로고    scopus 로고
    • Novel TUTase associates with an editosome-like complex in mitochondria of Trypanosoma brucei
    • Aphasizheva I., Ringpis G.E., Weng J., Gershon P.D., Lathrop R.H., Aphasizhev R. Novel TUTase associates with an editosome-like complex in mitochondria of Trypanosoma brucei. RNA 2009, 15:1322-1337.
    • (2009) RNA , vol.15 , pp. 1322-1337
    • Aphasizheva, I.1    Ringpis, G.E.2    Weng, J.3    Gershon, P.D.4    Lathrop, R.H.5    Aphasizhev, R.6
  • 20
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. Sect. D 2004, 60:2256-2268.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 21
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 22
    • 0034003595 scopus 로고    scopus 로고
    • The ATP-cone: an evolutionarily mobile, ATP-binding regulatory domain
    • Aravind L., Wolf Y.I., Koonin E.V. The ATP-cone: an evolutionarily mobile, ATP-binding regulatory domain. J. Mol. Microbiol. Biotechnol. 2000, 2:191-194.
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 191-194
    • Aravind, L.1    Wolf, Y.I.2    Koonin, E.V.3
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite-programs for protein crystallography
    • Bailey S. The CCP4 suite-programs for protein crystallography. Acta Crystallogr. Sect. D 1994, 50:760-763.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 24
    • 0141922994 scopus 로고    scopus 로고
    • Separate insertion and deletion subcomplexes of the Trypanosoma brucei RNA editing complex
    • Schnaufer A., Ernst N.L., Palazzo S.S., O'Rear J., Salavati R., Stuart K. Separate insertion and deletion subcomplexes of the Trypanosoma brucei RNA editing complex. Mol. Cell 2003, 12:307-319.
    • (2003) Mol. Cell , vol.12 , pp. 307-319
    • Schnaufer, A.1    Ernst, N.L.2    Palazzo, S.S.3    O'Rear, J.4    Salavati, R.5    Stuart, K.6
  • 25
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions 4
    • Wallace A.C., Laskowski R.A., Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions 4. Protein Eng. 1995, 8:127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 26
    • 27144545842 scopus 로고    scopus 로고
    • RNA uridylyltransferases
    • Aphasizhev R. RNA uridylyltransferases. Cell Mol. Life Sci. 2005, 62:2194-2203.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 2194-2203
    • Aphasizhev, R.1
  • 27
    • 33746489955 scopus 로고    scopus 로고
    • Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase
    • Trippe R., Guschina E., Hossbach M., Urlaub H., Luhrmann R., Benecke B.J. Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase. RNA 2006, 12:1494-1504.
    • (2006) RNA , vol.12 , pp. 1494-1504
    • Trippe, R.1    Guschina, E.2    Hossbach, M.3    Urlaub, H.4    Luhrmann, R.5    Benecke, B.J.6
  • 28
    • 38149023239 scopus 로고    scopus 로고
    • Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'
    • Mullen T.E., Marzluff W.F. Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Genes Dev. 2008, 22:50-65.
    • (2008) Genes Dev. , vol.22 , pp. 50-65
    • Mullen, T.E.1    Marzluff, W.F.2
  • 29
    • 68749102148 scopus 로고    scopus 로고
    • TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation
    • Heo I., Joo C., Kim Y.K., Ha M., Yoon M.J., Cho J., et al. TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation. Cell 2009, 138:696-708.
    • (2009) Cell , vol.138 , pp. 696-708
    • Heo, I.1    Joo, C.2    Kim, Y.K.3    Ha, M.4    Yoon, M.J.5    Cho, J.6
  • 30
    • 66849122924 scopus 로고    scopus 로고
    • Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA turnover
    • Rissland O.S., Norbury C.J. Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA turnover. Nat. Struct. Mol. Biol. 2009, 16:616-623.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 616-623
    • Rissland, O.S.1    Norbury, C.J.2
  • 31
    • 19644400971 scopus 로고    scopus 로고
    • Uridine addition after microRNA-directed cleavage
    • Shen B., Goodman H.M. Uridine addition after microRNA-directed cleavage. Science 2004, 306:997.
    • (2004) Science , vol.306 , pp. 997
    • Shen, B.1    Goodman, H.M.2
  • 32
    • 70349820140 scopus 로고    scopus 로고
    • Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells
    • Hagan J.P., Piskounova E., Gregory R.I. Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells. Nat. Struct. Mol. Biol. 2009, 16:1021-1025.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1021-1025
    • Hagan, J.P.1    Piskounova, E.2    Gregory, R.I.3
  • 36
    • 34248225381 scopus 로고    scopus 로고
    • Efficient RNA polyuridylation by noncanonical poly(A) polymerases
    • Rissland O.S., Mikulasova A., Norbury C.J. Efficient RNA polyuridylation by noncanonical poly(A) polymerases. Mol. Cell Biol. 2007, 27:3612-3624.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 3612-3624
    • Rissland, O.S.1    Mikulasova, A.2    Norbury, C.J.3
  • 38
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. Sect. D 2000, 56:965-972.
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 39
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger T.C. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. Sect. D 2003, 59:38-44.
    • (2003) Acta Crystallogr. Sect. D , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 40
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building: 1. Tracing protein chains
    • Cowtan K. The Buccaneer software for automated model building: 1. Tracing protein chains. Acta Crystallogr. Sect. D 2006, 62:1002-1011.
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 1002-1011
    • Cowtan, K.1


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