메뉴 건너뛰기




Volumn 16, Issue 5, 2010, Pages 1018-1031

Mutational analyses of trimethylguanosine synthase (Tgs1) and Mud2: Proteins implicated in pre-mRNA splicing

Author keywords

Methyltransferase; RRM domain; snRNPs; TMG caps

Indexed keywords

GUANOSINE DERIVATIVE; LYSINE; MESSENGER RNA; MUD2 PROTEIN; POLYPEPTIDE; PROTEIN DERIVATIVE; TRIMETHYLGUANOSINE SYNTHASE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 77951154264     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2082610     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0030911051 scopus 로고    scopus 로고
    • Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals
    • Abovich N, Rosbash M. 1997. Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell 89: 403-412.
    • (1997) Cell , vol.89 , pp. 403-412
    • Abovich, N.1    Rosbash, M.2
  • 2
    • 0028273768 scopus 로고
    • The yeast MUD2 protein: An interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition
    • Abovich N, Liao XC, Rosbash M. 1994. The yeast MUD2 protein: An interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition. Genes & Dev 8: 843-854.
    • (1994) Genes & Dev , vol.8 , pp. 843-854
    • Abovich, N.1    Liao, X.C.2    Rosbash, M.3
  • 3
    • 62549107067 scopus 로고    scopus 로고
    • Characterization of a mimivirus RNA cap guanine-N2 methyltransferase
    • Benarroch D, Qiu ZR, Schwer B, Shuman S. 2009. Characterization of a mimivirus RNA cap guanine-N2 methyltransferase. RNA 15: 666-674.
    • (2009) RNA , vol.15 , pp. 666-674
    • Benarroch, D.1    Qiu, Z.R.2    Schwer, B.3    Shuman, S.4
  • 4
    • 75649144466 scopus 로고    scopus 로고
    • Cap analog substrates reveal three clades of cap guanine-N2 methyltransferases with distinct methyl acceptor specificities
    • Benarroch D, Jankowska-Anyszka M, Stepinski J, Darzynkiewicz E, Shuman S. 2010. Cap analog substrates reveal three clades of cap guanine-N2 methyltransferases with distinct methyl acceptor specificities. RNA 16: 211-220.
    • (2010) RNA , vol.16 , pp. 211-220
    • Benarroch, D.1    Jankowska-Anyszka, M.2    Stepinski, J.3    Darzynkiewicz, E.4    Shuman, S.5
  • 5
    • 0032521186 scopus 로고    scopus 로고
    • A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition
    • Berglund JA, Abovich N, Rosbash M. 1998. A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition. Genes & Dev 12: 858-867.
    • (1998) Genes & Dev , vol.12 , pp. 858-867
    • Berglund, J.A.1    Abovich, N.2    Rosbash, M.3
  • 9
    • 14244264414 scopus 로고    scopus 로고
    • Specificity and mechanism of RNA cap guanine-N2 methyltransferase (Tgs1)
    • DOI 10.1074/jbc.C400554200
    • Hausmann S, Shuman S. 2005a. Specificity and mechanism of RNA cap guanine-N2 methyltransferase (Tgs1). J Biol Chem 280: 4021-4024. (Pubitemid 40288564)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4021-4024
    • Hausmann, S.1    Shuman, S.2
  • 10
    • 25444482810 scopus 로고    scopus 로고
    • Giardia lamblia RNA cap guanine-N2 methyltransferase (Tgs2)
    • DOI 10.1074/jbc.M506438200
    • Hausmann S, Shuman S. 2005b. Giardia lamblia RNA cap guanine-N2 methyltransferase (Tgs2). J Biol Chem 280: 32101-32106. (Pubitemid 41361815)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32101-32106
    • Hausmann, S.1    Shuman, S.2
  • 11
    • 34247152861 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe
    • Hausmann S, Ramirez A, Schneider S, Schwer B, Shuman S. 2007. Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe. Nucleic Acids Res 35: 1411-1420.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1411-1420
    • Hausmann, S.1    Ramirez, A.2    Schneider, S.3    Schwer, B.4    Shuman, S.5
  • 12
    • 57649120781 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of yeast and human cap trimethylguanosine synthase: Functional overlap of TMG caps, snRNP components, pre-mRNA splicing factors, and RNA decay pathways
    • Hausmann S, Zheng S, Costanzo M, Brost RL, Garcin D, Boone C, Shuman S, Schwer B. 2008. Genetic and biochemical analysis of yeast and human cap trimethylguanosine synthase: Functional overlap of TMG caps, snRNP components, pre-mRNA splicing factors, and RNA decay pathways. J Biol Chem 283: 31706-31718.
    • (2008) J Biol Chem , vol.283 , pp. 31706-31718
    • Hausmann, S.1    Zheng, S.2    Costanzo, M.3    Brost, R.L.4    Garcin, D.5    Boone, C.6    Shuman, S.7    Schwer, B.8
  • 14
    • 0037129933 scopus 로고    scopus 로고
    • The 'cap-binding' slot of an mRNA cap-binding protein: Quantitative effects of aromatic side chain choice in the double-stacking sandwich with cap
    • Hu G, Oguro A, Li C, Gershon PD, Quiocho FA. 2002. The 'cap-binding' slot of an mRNA cap-binding protein: Quantitative effects of aromatic side chain choice in the double-stacking sandwich with cap. Biochemistry 41: 7677-7687.
    • (2002) Biochemistry , vol.41 , pp. 7677-7687
    • Hu, G.1    Oguro, A.2    Li, C.3    Gershon, P.D.4    Quiocho, F.A.5
  • 15
    • 3042737403 scopus 로고    scopus 로고
    • U2AF homology motifs: Protein recognition in the RRM world
    • Kielkopf CL, Lücke S, Green MR. 2004. U2AF homology motifs: Protein recognition in the RRM world. Genes & Dev 18: 1513-1526.
    • (2004) Genes & Dev , vol.18 , pp. 1513-1526
    • Kielkopf, C.L.1    Lücke, S.2    Green, M.R.3
  • 16
    • 16844364934 scopus 로고    scopus 로고
    • DTL, the Drosophila homolog of PIMT/Tgs1 nuclear receptor coactivator-interacting protein/RNA methyltransferase, has an essential role in development
    • Komonyi O, Papai G, Enunlu I, Muratoglu S, Pankotai T, Kopitova D, Maró y P, Udvarty A, Boros I. 2005. DTL, the Drosophila homolog of PIMT/Tgs1 nuclear receptor coactivator-interacting protein/RNA methyltransferase, has an essential role in development. J Biol Chem 280: 12397-12404.
    • (2005) J Biol Chem , vol.280 , pp. 12397-12404
    • Komonyi, O.1    Papai, G.2    Enunlu, I.3    Muratoglu, S.4    Pankotai, T.5    Kopitova, D.6    Maróy, P.7    Udvarty, A.8    Boros, I.9
  • 18
    • 0027241224 scopus 로고
    • An enhancer screen identifies a gene that encodes the yeast U1 snRNP a protein: Implications for snRNP protein function in pre-mRNA splicing
    • Liao XC, Tang J, Rosbash M. 1993. An enhancer screen identifies a gene that encodes the yeast U1 snRNP A protein: Implications for snRNP protein function in pre-mRNA splicing. Genes & Dev 7: 419-428.
    • (1993) Genes & Dev , vol.7 , pp. 419-428
    • Liao, X.C.1    Tang, J.2    Rosbash, M.3
  • 19
    • 0023047717 scopus 로고
    • Cap trimethylation of U snRNA is cytoplasmic and dependent of U snRNP protein binding
    • Mattaj IW. 1986. Cap trimethylation of U snRNA is cytoplasmic and dependent of U snRNP protein binding. Cell 46: 905-911.
    • (1986) Cell , vol.46 , pp. 905-911
    • Mattaj, I.W.1
  • 20
    • 0037107401 scopus 로고    scopus 로고
    • 7GpppG cap analogue by the human nuclear cap-binding complex
    • DOI 10.1093/emboj/cdf538
    • Mazza C, Segref A, Mattaj IW, Cusack S. 2002. Large-scale induced fit recognition of an m7GpppG cap analogue by the human nuclear cap-binding complex. EMBO J 21: 5548-5557. (Pubitemid 35231034)
    • (2002) EMBO Journal , vol.21 , Issue.20 , pp. 5548-5557
    • Mazza, C.1    Segref, A.2    Mattaj, I.W.3    Cusack, S.4
  • 21
    • 0037980050 scopus 로고    scopus 로고
    • Spatial organization of protein-RNA interactions in the branch site-3′ splice site region during pre-mRNA splicing in yeast
    • McPheeters DS, Muhlenkamp P. 2003. Spatial organization of protein-RNA interactions in the branch site-3′ splice site region during pre-mRNA splicing in yeast. Mol Cell Biol 23: 4174-4186.
    • (2003) Mol Cell Biol , vol.23 , pp. 4174-4186
    • McPheeters, D.S.1    Muhlenkamp, P.2
  • 22
    • 0029745052 scopus 로고    scopus 로고
    • Cation-p interactions in aromatics of biological and medicinal interest: Electrostatic potential surfaces as a useful qualitative guide
    • Mecozzi S, West AP, Dougherty DA. 1996. Cation-p interactions in aromatics of biological and medicinal interest: Electrostatic potential surfaces as a useful qualitative guide. Proc Natl Acad Sci 93: 10566-10571.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 10566-10571
    • Mecozzi, S.1    West, A.P.2    Dougherty, D.A.3
  • 23
    • 51249098499 scopus 로고    scopus 로고
    • Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m7G-cap-binding mode
    • Monecke T, Schell S, Dickmanns, Ficner R. 2008. Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m7G-cap-binding mode. J Mol Biol 382: 827-834.
    • (2008) J Mol Biol , vol.382 , pp. 827-834
    • Monecke, T.1    Schell, S.2    Dickmanns, F.R.3
  • 24
    • 67651159060 scopus 로고    scopus 로고
    • 7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1
    • 7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1. Nucleic Acids Res 37: 3865-3877.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3865-3877
    • Monecke, T.1    Dickmanns, F.R.2
  • 25
    • 0036238278 scopus 로고    scopus 로고
    • Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus
    • Mouaikel J, Verheggen C, Bertrand E, Tazi J, Bordonné R. 2002. Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus. Mol Cell 9: 891-901.
    • (2002) Mol Cell , vol.9 , pp. 891-901
    • Mouaikel, J.1    Verheggen, C.2    Bertrand, E.3    Tazi, J.4    Bordonné, R.5
  • 26
    • 0344012478 scopus 로고    scopus 로고
    • Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase
    • Mouaikel J, Bujnicki JM, Tazi J, Bordonné R. 2003. Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase. Nucleic Acids Res 31: 4899-4909.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4899-4909
    • Mouaikel, J.1    Bujnicki, J.M.2    Tazi, J.3    Bordonné, R.4
  • 28
    • 0028176685 scopus 로고
    • M3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: Evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP protein that requires a binding site on the Sm core domain
    • Plessel G, Fischer U, Lührmann R. 1994. m3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: Evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP protein that requires a binding site on the Sm core domain. Mol Cell Biol 14: 4160-4172.
    • (1994) Mol Cell Biol , vol.14 , pp. 4160-4172
    • Plessel, G.1    Fischer, U.2    Lührmann, R.3
  • 29
    • 0031958545 scopus 로고    scopus 로고
    • Conservation of functional domains involved in RNA binding and protein-protein interactions in human and Saccharomyces cerevisiae pre-mRNA splicing factor SF1
    • Rain JC, Rafi Z, Legrain P, Krämer A. 1998. Conservation of functional domains involved in RNA binding and protein-protein interactions in human and Saccharomyces cerevisiae pre-mRNA splicing factor SF1. RNA 4: 551-565.
    • (1998) RNA , vol.4 , pp. 551-565
    • Rain, J.C.1    Rafi, Z.2    Legrain, P.3    Krämer, A.4
  • 30
    • 0345593813 scopus 로고    scopus 로고
    • Transient interaction of BBP/ScSF1 and Mud2 with the splicing machinery affects the kinetics of spliceosome assembly
    • Rutz B, Seraphin B. 1999. Transient interaction of BBP/ScSF1 and Mud2 with the splicing machinery affects the kinetics of spliceosome assembly. RNA 5: 819-831.
    • (1999) RNA , vol.5 , pp. 819-831
    • Rutz, B.1    Seraphin, B.2
  • 31
    • 0038298868 scopus 로고    scopus 로고
    • Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/BBP
    • Selenko P, Gregorovic G, Sprangers R, Stier G, Rhani Z, Krämer A, Sattler M. 2003. Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/BBP. Mol Cell 11: 965-976.
    • (2003) Mol Cell , vol.11 , pp. 965-976
    • Selenko, P.1    Gregorovic, G.2    Sprangers, R.3    Stier, G.4    Rhani, Z.5    Krämer, A.6    Sattler, M.7
  • 32
    • 33745499067 scopus 로고    scopus 로고
    • Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65
    • Sickmier EA, Frato KE, Shen H, Paranawithana SR, Green MR, Kielkopf CL. 2006. Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65. Mol Cell 23: 49-59.
    • (2006) Mol Cell , vol.23 , pp. 49-59
    • Sickmier, E.A.1    Frato, K.E.2    Shen, H.3    Paranawithana, S.R.4    Green, M.R.5    Kielkopf, C.L.6
  • 36
    • 0037438318 scopus 로고    scopus 로고
    • Disruption of 12 ORFs located on chromosomes IV, VIIA, and XIV of Saccharomyces cerevisiae reveals two essential genes
    • Volckaert G, Voet M, Van der Schueren J, Robben J, Vanstreels E. 2003. Disruption of 12 ORFs located on chromosomes IV, VIIA, and XIV of Saccharomyces cerevisiae reveals two essential genes. Yeast 20: 79-88.
    • (2003) Yeast , vol.20 , pp. 79-88
    • Volckaert, G.1    Voet, M.2    Van Der Schueren, J.3    Robben, J.4    Vanstreels, E.5
  • 37
    • 43349094305 scopus 로고    scopus 로고
    • A BBP-Mud2p heterodimer mediates branchpoint recognition and influences splicing substrate abundance in budding yeast
    • Wang Q, Zhang L, Lynn B, Rymond BC. 2008. A BBP-Mud2p heterodimer mediates branchpoint recognition and influences splicing substrate abundance in budding yeast. Nucleic Acids Res 36: 2787-2798.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2787-2798
    • Wang, Q.1    Zhang, L.2    Lynn, B.3    Rymond, B.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.