메뉴 건너뛰기




Volumn 66, Issue , 2000, Pages 1-40

Structure, mechanism, and evolution of the mRNA capping apparatus

Author keywords

[No Author keywords available]

Indexed keywords

ACID ANHYDRIDE HYDROLASE; CAP I RNA (NUCLEOSIDE 2' )METHYLTRANSFERASE; CAP I RNA (NUCLEOSIDE-2'-)METHYLTRANSFERASE; CAP II RNA(NUCLEOSIDE 2' )METHYLTRANSFERASE; CAP II RNA(NUCLEOSIDE-2'-)METHYLTRANSFERASE; CAPPED RNA; FUNGAL PROTEIN; MESSENGER RIBONUCLEIC ACID GUANYLYLTRANSFERASE; MESSENGER RNA; METHYLTRANSFERASE; NUCLEOTIDYLTRANSFERASE; RNA TRIPHOSPHATASE;

EID: 0035201941     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0079-6603(00)66025-7     Document Type: Review
Times cited : (263)

References (89)
  • 1
    • 0029107231 scopus 로고
    • Capping enzyme in eukaryotic mRNA synthesis
    • S Shuman Capping enzyme in eukaryotic mRNA synthesis Prog. Nucleic Acid Res. Mol. Biol 50 1995 101 129
    • (1995) Prog. Nucleic Acid Res. Mol. Biol , vol.50 , pp. 101-129
    • Shuman, S1
  • 2
    • 0026733001 scopus 로고
    • mRNA capping enzyme: isolation and characterization of the gene encoding mRNA guanylyltransferase subunit from Saccharomyces cerevisiae
    • Y Shibagaki N Itoh H Yamada S Hagata K Mizumoto mRNA capping enzyme: isolation and characterization of the gene encoding mRNA guanylyltransferase subunit from Saccharomyces cerevisiae J. Biol. Chem 267 1992 9521 9528
    • (1992) J. Biol. Chem , vol.267 , pp. 9521-9528
    • Shibagaki, Y1    Itoh, N2    Yamada, H3    Hagata, S4    Mizumoto, K5
  • 3
    • 0028211258 scopus 로고
    • Mutational analysis of yeast mRNA capping enzyme
    • B Schwer S Shuman Mutational analysis of yeast mRNA capping enzyme 6th ed. Proc. Nod. Acad. Sci. USA 91 1994 4328 4332
    • (1994) , pp. 4328-4332
    • Schwer, B1    Shuman, S2
  • 4
    • 0028172876 scopus 로고
    • Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and vaccinia capping enzymes and among DNA ligases
    • S Shuman Y Liu B Schwer Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and vaccinia capping enzymes and among DNA ligases 6th ed. Proc. Nad. Acad. Sci. USA 91 1994 12046 12050
    • (1994) , pp. 12046-12050
    • Shuman, S1    Liu, Y2    Schwer, B3
  • 5
    • 0028214041 scopus 로고
    • Active site of the mRNA capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases
    • L.D Fresco S Buratowski Active site of the mRNA capping enzyme guanylyltransferase from Saccharomyces cerevisiae : similarity to the nucleotidyl attachment motif of DNA and RNA ligases 6th ed. Proc. Nad. Acad. Sci. USA 91 1994 6624 6628
    • (1994) , pp. 6624-6628
    • Fresco, L.D1    Buratowski, S2
  • 6
    • 0029558314 scopus 로고
    • Location and in vitro mutagenesis of the active site in the Saccharomyces cerevisiae mRNA capping enzyme
    • Y Shibagaki H Gotoh M Kato K Mizumoto Location and in vitro mutagenesis of the active site in the Saccharomyces cerevisiae mRNA capping enzyme J. Biochem. (Tokyo) 118 1995 1303 1309
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 1303-1309
    • Shibagaki, Y1    Gotoh, H2    Kato, M3    Mizumoto, K4
  • 7
    • 0029951308 scopus 로고    scopus 로고
    • Conditional mutants of the yeast mRNA capping enzyme show that the cap enhances, but is not required for, mRNA splicing
    • L.D Fresco S Buratowski Conditional mutants of the yeast mRNA capping enzyme show that the cap enhances, but is not required for, mRNA splicing RNA 2 1996 584 596
    • (1996) RNA , vol.2 , pp. 584-596
    • Fresco, L.D1    Buratowski, S2
  • 8
    • 0032077454 scopus 로고    scopus 로고
    • Accelerated mRNA decay in conditional mutants of yeast mRNA capping enzyme
    • B Schwer X Mao S Shuman Accelerated mRNA decay in conditional mutants of yeast mRNA capping enzyme Nucleic Acids Res 26 1998 2050 2057
    • (1998) Nucleic Acids Res , vol.26 , pp. 2050-2057
    • Schwer, B1    Mao, X2    Shuman, S3
  • 9
    • 0029902842 scopus 로고    scopus 로고
    • Conditional inactivation of mRNA capping enzyme affects premRNA splicing in vivo
    • B Schwer S Shuman Conditional inactivation of mRNA capping enzyme affects premRNA splicing in vivo RNA 2 1996 574 583
    • (1996) RNA , vol.2 , pp. 574-583
    • Schwer, B1    Shuman, S2
  • 10
    • 0029001790 scopus 로고
    • Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene
    • X Mao B Schwer S Shuman Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene Mol. Cell. Biol. 15 1995 4167 4174
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4167-4174
    • Mao, X1    Schwer, B2    Shuman, S3
  • 11
    • 0031561370 scopus 로고    scopus 로고
    • Isolation and characterization of the yeast mRNA capping enzyme β subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability
    • T Tsukamoto Y Shibagaki S Imajoh-Ohmi T Murakoshi M Suzuki A Nakamura H Gotoh K Mizumoto Isolation and characterization of the yeast mRNA capping enzyme β subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability Biochem. Biophys. Res. Comm. 239 1997 116 122
    • (1997) Biochem. Biophys. Res. Comm. , vol.239 , pp. 116-122
    • Tsukamoto, T1    Shibagaki, Y2    Imajoh-Ohmi, S3    Murakoshi, T4    Suzuki, M5    Nakamura, A6    Gotoh, H7    Mizumoto, K8
  • 12
    • 3543026832 scopus 로고    scopus 로고
    • Genetic, physical and function interactions between the triphosphatase and gunaylyltransferase components of the yeast mRNA capping apparatus
    • C.K Ho B Schwer S Shuman Genetic, physical and function interactions between the triphosphatase and gunaylyltransferase components of the yeast mRNA capping apparatus Mol. Cell. Biol. 18 1998 5189 5198
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5189-5198
    • Ho, C.K1    Schwer, B2    Shuman, S3
  • 13
    • 0032545284 scopus 로고    scopus 로고
    • Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family
    • C.K Ho Y Pei S Shuman Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family J. Biol. Chem. 273 1998 34151 34156
    • (1998) J. Biol. Chem. , vol.273 , pp. 34151-34156
    • Ho, C.K1    Pei, Y2    Shuman, S3
  • 14
    • 0030060410 scopus 로고    scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap methyltransferase activity is essential for cell growth
    • X Mao B Schwer S Shuman Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap methyltransferase activity is essential for cell growth Mol. Cell. Biol. 16 1996 475 1180
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 475-1180
    • Mao, X1    Schwer, B2    Shuman, S3
  • 15
    • 0000643270 scopus 로고    scopus 로고
    • Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae
    • S.P Wang S Shuman Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae J. Biol. Chem. 272 1997 14683 14689
    • (1997) J. Biol. Chem. , vol.272 , pp. 14683-14689
    • Wang, S.P1    Shuman, S2
  • 16
    • 0033522898 scopus 로고    scopus 로고
    • Characterization of human, Schizosaccharomyces pombe and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes
    • N Saha B Schwer S Shuman Characterization of human, Schizosaccharomyces pombe and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes J. Biol. Chem. 274 1999 16553 16562
    • (1999) J. Biol. Chem. , vol.274 , pp. 16553-16562
    • Saha, N1    Schwer, B2    Shuman, S3
  • 17
    • 0033529501 scopus 로고    scopus 로고
    • A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus
    • K Lehman B Schwer C.K Ho I Rouzankina S Shuman A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus J. Biol. Chem. 274 1999 22668 22678
    • (1999) J. Biol. Chem. , vol.274 , pp. 22668-22678
    • Lehman, K1    Schwer, B2    Ho, C.K3    Rouzankina, I4    Shuman, S5
  • 18
    • 0029764473 scopus 로고    scopus 로고
    • Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans
    • T Yamada-Okabe O Shimmi R Doi K Mizumoto M Arisawa H Yamada-Okabe Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans Microbiology 142 1996 2515 2523
    • (1996) Microbiology , vol.142 , pp. 2515-2523
    • Yamada-Okabe, T1    Shimmi, O2    Doi, R3    Mizumoto, K4    Arisawa, M5    Yamada-Okabe, H6
  • 19
    • 0032508492 scopus 로고    scopus 로고
    • Isolation and characterization of the Candida albicans gene for mRNA 5′ triphosphatase: association of mRNA 5′ triphosphatase and mRNA 5′ guanylyltransferase activities is essential for the function of mRNA 5′ capping enzyme in vivo
    • T Yamada-Okabe T Mio M Matsui Y Kashima M Arisawa H Yamada-Okabe Isolation and characterization of the Candida albicans gene for mRNA 5′ triphosphatase: association of mRNA 5′ triphosphatase and mRNA 5′ guanylyltransferase activities is essential for the function of mRNA 5′ capping enzyme in vivo FEBS Lett 435 1998 49 54
    • (1998) FEBS Lett , vol.435 , pp. 49-54
    • Yamada-Okabe, T1    Mio, T2    Matsui, M3    Kashima, Y4    Arisawa, M5    Yamada-Okabe, H6
  • 20
    • 0030660264 scopus 로고    scopus 로고
    • Mammalian capping enzyme complements mutant S. cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
    • Z Yue E Maldonado R Pillutla H Cho D Reinberg A.J Shatkin Mammalian capping enzyme complements mutant S. cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II 6th ed. Proc. Nad. Acad. Sci. USA 94 1997 12898 12903
    • (1997) , pp. 12898-12903
    • Yue, Z1    Maldonado, E2    Pillutla, R3    Cho, H4    Reinberg, D5    Shatkin, A.J6
  • 22
    • 0032540231 scopus 로고    scopus 로고
    • The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • C.K Ho V Sriskanda S McCracken D Bentley B Schwer S Shuman The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II J. Biol. Chem. 273 1998 9577 9585
    • (1998) J. Biol. Chem. , vol.273 , pp. 9577-9585
    • Ho, C.K1    Sriskanda, V2    McCracken, S3    Bentley, D4    Schwer, B5    Shuman, S6
  • 23
    • 0032052285 scopus 로고    scopus 로고
    • Isolation and characterization of a human cDNA for mRNA 5′-capping enzyme
    • T Yamada-Okabe R Doi O Shimmi M Arisawa H Yamada-Okabe Isolation and characterization of a human cDNA for mRNA 5′-capping enzyme Nucleic Acids Res 26 1998 1700 1706
    • (1998) Nucleic Acids Res , vol.26 , pp. 1700-1706
    • Yamada-Okabe, T1    Doi, R2    Shimmi, O3    Arisawa, M4    Yamada-Okabe, H5
  • 25
    • 0032555486 scopus 로고    scopus 로고
    • Recombinant human mRNA cap methyltransferase hinds capping enzyme/RNA polymerise Ho complexes
    • R.C Pillutla Z Yoe E Maldonado A.J Shatkin Recombinant human mRNA cap methyltransferase hinds capping enzyme/RNA polymerise Ho complexes J. Biol. Chem. 273 1998 21443 21446
    • (1998) J. Biol. Chem. , vol.273 , pp. 21443-21446
    • Pillutla, R.C1    Yoe, Z2    Maldonado, E3    Shatkin, A.J4
  • 26
    • 0032500741 scopus 로고    scopus 로고
    • Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase
    • T Tsukamoto Y Shibagaki Y Niikura K Mizumoto Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase Biochem. Biophys. Res. Comm. 251 1998 27 34
    • (1998) Biochem. Biophys. Res. Comm. , vol.251 , pp. 27-34
    • Tsukamoto, T1    Shibagaki, Y2    Niikura, Y3    Mizumoto, K4
  • 27
    • 0029903010 scopus 로고    scopus 로고
    • Domain structure of the vaccinia virus mRNA capping enzyme: expression in Escherichia coli of a subdomain possessing the RNA 5′-triphosphatase and guanylyltransferase activities and a kinetic comparison to the full-size enzyme
    • J Myette E.G Niles Domain structure of the vaccinia virus mRNA capping enzyme: expression in Escherichia coli of a subdomain possessing the RNA 5′-triphosphatase and guanylyltransferase activities and a kinetic comparison to the full-size enzyme J. Biol. Chem. 271 1996 11936 11944
    • (1996) J. Biol. Chem. , vol.271 , pp. 11936-11944
    • Myette, J1    Niles, E.G2
  • 28
    • 0030007647 scopus 로고    scopus 로고
    • Characterization of the vaccinia virus RNA 5′-triphosphatase and nucleoside triphosphate phosphohydrolase activities: demonstration that both activities are carried out at the same active site
    • J Myette E.G Niles Characterization of the vaccinia virus RNA 5′-triphosphatase and nucleoside triphosphate phosphohydrolase activities: demonstration that both activities are carried out at the same active site J. Biol. Chem. 271 1996 11945 11952
    • (1996) J. Biol. Chem. , vol.271 , pp. 11945-11952
    • Myette, J1    Niles, E.G2
  • 29
    • 0029793256 scopus 로고    scopus 로고
    • Mutational analysis of the triphosphatase domain of vaccinia virus mRNA capping enzyme
    • L Yu S Shuman Mutational analysis of the triphosphatase domain of vaccinia virus mRNA capping enzyme J. Virol. 70 1996 6162 6168
    • (1996) J. Virol. , vol.70 , pp. 6162-6168
    • Yu, L1    Shuman, S2
  • 30
    • 0030728958 scopus 로고    scopus 로고
    • Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme
    • L Yu A Martins L Deng S Shuman Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme J. Virol 71 1997 9837 9843
    • (1997) J. Virol , vol.71 , pp. 9837-9843
    • Yu, L1    Martins, A2    Deng, L3    Shuman, S4
  • 31
    • 0031772992 scopus 로고    scopus 로고
    • RNA 5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculovirus LEF-4 protein
    • C.H Gross S Shuman RNA 5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculovirus LEF-4 protein J. Virol. 72 1998 10020 10028
    • (1998) J. Virol. , vol.72 , pp. 10020-10028
    • Gross, C.H1    Shuman, S2
  • 32
    • 0031775225 scopus 로고    scopus 로고
    • The LEF-4 subunit of baculovirus RNA polymerase has RNA 5′-triphosphatase and ATPase activities
    • E Jin W Dong L.A Guarino The LEF-4 subunit of baculovirus RNA polymerase has RNA 5′-triphosphatase and ATPase activities J. Virol. 72 1998 10011 10019
    • (1998) J. Virol. , vol.72 , pp. 10011-10019
    • Jin, E1    Dong, W2    Guarino, L.A3
  • 33
    • 0030680252 scopus 로고    scopus 로고
    • Origins of mRNA identity: capping enzymes hind to the phosphorylated C-terminal domain of RNA polymerase II
    • S Shuman Origins of mRNA identity: capping enzymes hind to the phosphorylated C-terminal domain of RNA polymerase II 6th ed. Proc. Nad. Acid. Sci. USA 94 1997 12758 12760
    • (1997) , pp. 12758-12760
    • Shuman, S1
  • 34
    • 0031453408 scopus 로고    scopus 로고
    • mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxyl-terminal domain
    • E Cho T Takagi C.R Moore S Buratowski mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxyl-terminal domain Genes Dev 11 1997 3319 3326
    • (1997) Genes Dev , vol.11 , pp. 3319-3326
    • Cho, E1    Takagi, T2    Moore, C.R3    Buratowski, S4
  • 35
    • 0032533898 scopus 로고    scopus 로고
    • Allosteric interactions between capping enzyme subunits and the RNA polymerase 11 carboxyl-terminal domain
    • E Cho C.R Rodriguez T Takagi S Buratowski Allosteric interactions between capping enzyme subunits and the RNA polymerase 11 carboxyl-terminal domain Genes. Dev. 12 1998 3482 3487
    • (1998) Genes. Dev. , vol.12 , pp. 3482-3487
    • Cho, E1    Rodriguez, C.R2    Takagi, T3    Buratowski, S4
  • 36
    • 0033105827 scopus 로고    scopus 로고
    • Distinct roles for CTD Ser2 and Ser5 phosphorylation in the recruitment and allosteric activation of mammalian capping enzyme
    • C.K Ho S Shuman Distinct roles for CTD Ser2 and Ser5 phosphorylation in the recruitment and allosteric activation of mammalian capping enzyme Mol. Cell 3 1999 405 411
    • (1999) Mol. Cell , vol.3 , pp. 405-411
    • Ho, C.K1    Shuman, S2
  • 37
    • 0017161004 scopus 로고
    • Modification of the 5′ terminus of mRNA by an RNA (guanine7-)-methyltransferase from HeLa cells
    • M.J Ensinger B Moss Modification of the 5′ terminus of mRNA by an RNA (guanine7-)-methyltransferase from HeLa cells J. Biol. Chem. 251 1976 5283 5291
    • (1976) J. Biol. Chem. , vol.251 , pp. 5283-5291
    • Ensinger, M.J1    Moss, B2
  • 38
    • 0000262312 scopus 로고
    • Mechanism of mRNA capping by vaccinia virus guanylyltransferase: characterization of an enzyme-guanylate intermediate
    • S Shuman J Hurwitz Mechanism of mRNA capping by vaccinia virus guanylyltransferase: characterization of an enzyme-guanylate intermediate 6th ed. Proc. Natl. Acid. Sci. USA 78 1981 187 191
    • (1981) , pp. 187-191
    • Shuman, S1    Hurwitz, J2
  • 39
    • 0029056990 scopus 로고
    • RNA capping enzyme and DNA ligase-a superfamily of covalent nucleotidyl transferases
    • S Shuman B Schwer RNA capping enzyme and DNA ligase-a superfamily of covalent nucleotidyl transferases Mol. Microbiol 17 1995 405 410
    • (1995) Mol. Microbiol , vol.17 , pp. 405-410
    • Shuman, S1    Schwer, B2
  • 40
    • 0000086141 scopus 로고    scopus 로고
    • Phylogeny of mRNA capping enzymes
    • S.P Wang L Deng C.K Ho S Shuman Phylogeny of mRNA capping enzymes 6th ed. Proc. Nad. Acid. Sci. USA 94 1997 9573 9578
    • (1997) , pp. 9573-9578
    • Wang, S.P1    Deng, L2    Ho, C.K3    Shuman, S4
  • 41
    • 0027408354 scopus 로고
    • Covalent catalysis in nucleotidyl transfer: a KTDG motif essential for enzyme-GMP complex formation by mRNA capping enzyme is conserved at the active sites of RNA and DNA ligases
    • P Cong S Shuman Covalent catalysis in nucleotidyl transfer: a KTDG motif essential for enzyme-GMP complex formation by mRNA capping enzyme is conserved at the active sites of RNA and DNA ligases J. Biol. Chem. 268 1993 7256 7260
    • (1993) J. Biol. Chem. , vol.268 , pp. 7256-7260
    • Cong, P1    Shuman, S2
  • 42
    • 0027424399 scopus 로고
    • Identification of the vaccinia virus mRNA guanylyltransferase active site lysine
    • E.G Niles L Christen Identification of the vaccinia virus mRNA guanylyltransferase active site lysine J. Biol. Chem. 268 1993 24986 24989
    • (1993) J. Biol. Chem. , vol.268 , pp. 24986-24989
    • Niles, E.G1    Christen, L2
  • 43
    • 0026011091 scopus 로고
    • Location of the active site for enzyme-adenylate formation in DNA ligases
    • A.E Tomkinson N.F Totty M Ginsburg T Lindahl Location of the active site for enzyme-adenylate formation in DNA ligases 6th ed. Proc. Nad. Acid. Sci. USA 88 1991 400 404
    • (1991) , pp. 400-404
    • Tomkinson, A.E1    Totty, N.F2    Ginsburg, M3    Lindahl, T4
  • 44
    • 0027970892 scopus 로고
    • Mammalian DNA ligase II is highly homologous with vaccinia DNA ligase: identification of the DNA ligase active site for enzyme-adenylate formation
    • Y.J Wang W.A Burkhart Z.B Mickey M.B Moyer W Ramos I Husain J Chen J.M Besterman A.E Tomkinson Mammalian DNA ligase II is highly homologous with vaccinia DNA ligase: identification of the DNA ligase active site for enzyme-adenylate formation J. Biol. Chem. 269 1994 31923 31928
    • (1994) J. Biol. Chem. , vol.269 , pp. 31923-31928
    • Wang, Y.J1    Burkhart, W.A2    Mickey, Z.B3    Moyer, M.B4    Ramos, W5    Husain, I6    Chen, J7    Besterman, J.M8    Tomkinson, A.E9
  • 45
    • 0028862970 scopus 로고
    • Mutational analysis of mRNA capping enzyme identifies amino acids involved in GTP binding, enzyme-guanylate complex formation, and GMP transfer to RNA
    • P Cong S Shuman Mutational analysis of mRNA capping enzyme identifies amino acids involved in GTP binding, enzyme-guanylate complex formation, and GMP transfer to RNA Mol. Cell. Biol. 15 1995 6222 6231
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6222-6231
    • Cong, P1    Shuman, S2
  • 46
    • 0029152217 scopus 로고
    • Mutational analysis of vaccinia DNA ligase defines residues essential for covalent catalysis
    • S Shuman X Ru Mutational analysis of vaccinia DNA ligase defines residues essential for covalent catalysis Virology 211 1995 73 83
    • (1995) Virology , vol.211 , pp. 73-83
    • Shuman, S1    Ru, X2
  • 47
    • 0032518177 scopus 로고    scopus 로고
    • Chlorella virus DNA ligase: nick recognition and mutational analysis
    • V Sriskanda S Shuman Chlorella virus DNA ligase: nick recognition and mutational analysis Nucleic Acids Res 26 1998 525 531
    • (1998) Nucleic Acids Res , vol.26 , pp. 525-531
    • Sriskanda, V1    Shuman, S2
  • 48
    • 0032531971 scopus 로고
    • Mutational analysis of Chlorella virus DNA ligase: catalytic roles of domain I and motif VI
    • V Sriskanda S Shuman Mutational analysis of Chlorella virus DNA ligase: catalytic roles of domain I and motif VI Nucleic Acids Res 26 1988 4618 4625
    • (1988) Nucleic Acids Res , vol.26 , pp. 4618-4625
    • Sriskanda, V1    Shuman, S2
  • 49
    • 0033570011 scopus 로고    scopus 로고
    • Mutational analysis of E. coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4
    • V Sriskanda B Schwer C.K Ho S Shuman Mutational analysis of E. coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4 Nucleic Acids Res 27 1999 3953 3963
    • (1999) Nucleic Acids Res , vol.27 , pp. 3953-3963
    • Sriskanda, V1    Schwer, B2    Ho, C.K3    Shuman, S4
  • 50
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • H.S Subramanya A.J Doherty S.R Ashford D.B Wigley Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7 Cell 85 1996 607 615
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S1    Doherty, A.J2    Ashford, S.R3    Wigley, D.B4
  • 51
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • K Hakansson A.J Doherty S Shuman D.B Wigley X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes Cell 89 1997 545 553
    • (1997) Cell , vol.89 , pp. 545-553
    • Hakansson, K1    Doherty, A.J2    Shuman, S3    Wigley, D.B4
  • 52
    • 0025833760 scopus 로고
    • Viruses and viruslike particles of eukaryotic algae
    • J.L Van Etten L.C Lane R.H Meints Viruses and viruslike particles of eukaryotic algae Microbiol. Rev. 55 1991 586 620
    • (1991) Microbiol. Rev. , vol.55 , pp. 586-620
    • Van Etten, J.L1    Lane, L.C2    Meints, R.H3
  • 53
    • 0029817880 scopus 로고    scopus 로고
    • Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1
    • C.K Ho J.L Van Etten S Shuman Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1 J. Virol 70 1996 6658 6664
    • (1996) J. Virol , vol.70 , pp. 6658-6664
    • Ho, C.K1    Van Etten, J.L2    Shuman, S3
  • 54
    • 0032539677 scopus 로고    scopus 로고
    • Structure of a complex between a cap analogue and mRNA guanylyltransferase demonstrates the structural chemistry of RNA capping
    • K Håkansson D.B Wigley Structure of a complex between a cap analogue and mRNA guanylyltransferase demonstrates the structural chemistry of RNA capping Proc. Natl. Acad. Sci. USA 95 1998 1505 1510
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1505-1510
    • Håkansson, K1    Wigley, D.B2
  • 55
    • 0033605569 scopus 로고    scopus 로고
    • Standard free energy for the hydrolysis of adenylylated T4 DNA ligase and the apparent pKa of lysine 159
    • A Arabshahi P.A Frey Standard free energy for the hydrolysis of adenylylated T4 DNA ligase and the apparent pKa of lysine 159 J. Biol. Chem. 272 1999 8586 8588
    • (1999) J. Biol. Chem. , vol.272 , pp. 8586-8588
    • Arabshahi, A1    Frey, P.A2
  • 56
    • 0033566722 scopus 로고    scopus 로고
    • Conversion of a DNA ligase into an RNA capping enzyme
    • A.J Doherty Conversion of a DNA ligase into an RNA capping enzyme Nucleic Acids Res 27 1999 3253 3258
    • (1999) Nucleic Acids Res , vol.27 , pp. 3253-3258
    • Doherty, A.J1
  • 57
    • 0033534370 scopus 로고    scopus 로고
    • Functional domains of an ATP-dependent DNA ligase
    • A.J Doherty D.B Wigley Functional domains of an ATP-dependent DNA ligase J. Mol. Biol. 285 1999 63 71
    • (1999) J. Mol. Biol. , vol.285 , pp. 63-71
    • Doherty, A.J1    Wigley, D.B2
  • 58
    • 0033534503 scopus 로고    scopus 로고
    • Functional domains of an NAD+-dependent DNA ligase
    • +-dependent DNA ligase J. Mol. Biol. 285 1999 73 83
    • (1999) J. Mol. Biol. , vol.285 , pp. 73-83
    • Timson, D.J1    Wigley, D.B2
  • 59
    • 0032514620 scopus 로고    scopus 로고
    • Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism
    • Y Wen Z Yue A.J Shatkin Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism 6th ed. Proc. Nail. Acad. Sci. USA 95 1998 12226 12231
    • (1998) , pp. 12226-12231
    • Wen, Y1    Yue, Z2    Shatkin, A.J3
  • 60
    • 0030807902 scopus 로고    scopus 로고
    • An RNA 5′-triphosphatase related to the protein tyrosine phosphatases
    • T Takagi C.R Moore F Diehn S Buratowski An RNA 5′-triphosphatase related to the protein tyrosine phosphatases Cell 89 1997 867 873
    • (1997) Cell , vol.89 , pp. 867-873
    • Takagi, T1    Moore, C.R2    Diehn, F3    Buratowski, S4
  • 61
    • 0032849895 scopus 로고    scopus 로고
    • Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus
    • Y Pei C.K Ho B Schwer S Shuman Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus J. Biol. Chem. 274 1999 28865 28874
    • (1999) J. Biol. Chem. , vol.274 , pp. 28865-28874
    • Pei, Y1    Ho, C.K2    Schwer, B3    Shuman, S4
  • 62
    • 0033601125 scopus 로고    scopus 로고
    • Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus
    • C Lima L.K Wang S Shuman Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus Cell 99 2000 533 543
    • (2000) Cell , vol.99 , pp. 533-543
    • Lima, C1    Wang, L.K2    Shuman, S3
  • 63
    • 0033562339 scopus 로고    scopus 로고
    • A Saccharomyces cerevisiae. RNA 5′-triphosphatase related to mRNA capping enzyme
    • C.R Rodriguez T Takagi E Cho S Buratowski A Saccharomyces cerevisiae . RNA 5′-triphosphatase related to mRNA capping enzyme Nucleic Acids. Res. 27 1999 2182 2188
    • (1999) Nucleic Acids. Res. , vol.27 , pp. 2182-2188
    • Rodriguez, C.R1    Takagi, T2    Cho, E3    Buratowski, S4
  • 64
    • 0033523023 scopus 로고    scopus 로고
    • Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5′-triphosphatase and diphosphatase activities
    • T Deshpande T Takagi L Hao S Buratowski H Charbonneau Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5′-triphosphatase and diphosphatase activities J. Biol. Chem. 274 1999 16590 16594
    • (1999) J. Biol. Chem. , vol.274 , pp. 16590-16594
    • Deshpande, T1    Takagi, T2    Hao, L3    Buratowski, S4    Charbonneau, H5
  • 65
    • 0031820701 scopus 로고    scopus 로고
    • Characterization of a baculovirus-encoded RNA 5′ triphosphatase
    • C.H Gross S Shuman Characterization of a baculovirus-encoded RNA 5′ triphosphatase J. Virol 72 1998 7057 7063
    • (1998) J. Virol , vol.72 , pp. 7057-7063
    • Gross, C.H1    Shuman, S2
  • 66
    • 0032544081 scopus 로고    scopus 로고
    • A protein-tyrosine phosphatase-like protein from baculovirus has RNA 5′-triphosphatase and diphosphatase activities
    • T Takagi L Hao H Charbonneau S Buratowski A protein-tyrosine phosphatase-like protein from baculovirus has RNA 5′-triphosphatase and diphosphatase activities 6th ed. Proc. Nail. Acad. Sci. USA 95 1998 9808 9812
    • (1998) , pp. 9808-9812
    • Takagi, T1    Hao, L2    Charbonneau, H3    Buratowski, S4
  • 67
    • 0029917244 scopus 로고    scopus 로고
    • Visualization of intermediate and transition state structures in protein tyrosine phosphatase catalysis
    • J.M Denu D.L Lohse J Vijayalakshmi M.A Saper J.E Dixon Visualization of intermediate and transition state structures in protein tyrosine phosphatase catalysis 6th ed. Proc. Natl. Acad. Sci. USA 93 1996 2493 2498
    • (1996) , pp. 2493-2498
    • Denu, J.M1    Lohse, D.L2    Vijayalakshmi, J3    Saper, M.A4    Dixon, J.E5
  • 68
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase IB
    • Z Jia D Barford A.J Flint N.K Tonks Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase IB Science 268 1995 1754 1757
    • (1995) Science , vol.268 , pp. 1754-1757
    • Jia, Z1    Barford, D2    Flint, A.J3    Tonks, N.K4
  • 69
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 113
    • D Barford A.J Flint N.K Tonks Crystal structure of human protein tyrosine phosphatase 113 Science 263 1994 1397 1404
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D1    Flint, A.J2    Tonks, N.K3
  • 70
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5Å and the complex with tungstate
    • J.A Stuckey H.L Schubert E.B Fauman X Zhang J.E Dixon M.A Saper Crystal structure of Yersinia protein tyrosine phosphatase at 2.5Å and the complex with tungstate Nature 370 1994 571 575
    • (1994) Nature , vol.370 , pp. 571-575
    • Stuckey, J.A1    Schubert, H.L2    Fauman, E.B3    Zhang, X4    Dixon, J.E5    Saper, M.A6
  • 71
    • 0028030520 scopus 로고
    • The crystal structure of a lowmolecular weight phosphotyrosine protein phosphatase
    • X Su N Taddel S Stefani G Ramponi P Norlund The crystal structure of a lowmolecular weight phosphotyrosine protein phosphatase Nature 370 1994 575 578
    • (1994) Nature , vol.370 , pp. 575-578
    • Su, X1    Taddel, N2    Stefani, S3    Ramponi, G4    Norlund, P5
  • 72
    • 0029780526 scopus 로고    scopus 로고
    • The X-ray crystal structure of Yersinia tyrosine phosphatase with bound tungstate and nitrate
    • E.B Fauman C Yuvaniyama H.L Schubert J.A Stuckey M.A Saper The X-ray crystal structure of Yersinia tyrosine phosphatase with bound tungstate and nitrate J. Biol. Chem. 271 1996 18780 18788
    • (1996) J. Biol. Chem. , vol.271 , pp. 18780-18788
    • Fauman, E.B1    Yuvaniyama, C2    Schubert, H.L3    Stuckey, J.A4    Saper, M.A5
  • 73
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • J Yuvaniyama J.M Denu J.E Dixon M.A Saper Crystal structure of the dual specificity protein phosphatase VHR Science 272 1996 1328 1331
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J1    Denu, J.M2    Dixon, J.E3    Saper, M.A4
  • 74
    • 0023654017 scopus 로고
    • Messenger RNA guanylyltransferase from Saccharomyces cerevisiae.: large scale purification, subunit functions, and subcellular localization
    • N Itch H Yamada Y Kaziro K Mizumoto Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. : large scale purification, subunit functions, and subcellular localization J. Biol. Chem. 262 1987 2989 2995
    • (1987) J. Biol. Chem. , vol.262 , pp. 2989-2995
    • Itch, N1    Yamada, H2    Kaziro, Y3    Mizumoto, K4
  • 75
    • 0033572891 scopus 로고    scopus 로고
    • An essential surface motif (WAQKW) of yeast RNA triphosphatase mediates formation of the mRNA capping enzyme complex with RNA guanylyltransferase
    • C.K Ho K Lehman S Shuman An essential surface motif (WAQKW) of yeast RNA triphosphatase mediates formation of the mRNA capping enzyme complex with RNA guanylyltransferase Nucleic Acids. Res. 27 1999 4671 4678
    • (1999) Nucleic Acids. Res. , vol.27 , pp. 4671-4678
    • Ho, C.K1    Lehman, K2    Shuman, S3
  • 76
    • 0027154080 scopus 로고
    • A protein phosphatase related to the vaccinia virus VH1 is encoded in the genomes of several ortbopoxviruses and a baculovirus
    • D.J Hakes K.J Martell W.G Zhao R.F Massung J.J Esposito J.E Dixon A protein phosphatase related to the vaccinia virus VH1 is encoded in the genomes of several ortbopoxviruses and a baculovirus 6th ed. Proc. Natl. Acad. Sci. USA 90 1993 4017 4021
    • (1993) , pp. 4017-4021
    • Hakes, D.J1    Martell, K.J2    Zhao, W.G3    Massung, R.F4    Esposito, J.J5    Dixon, J.E6
  • 77
    • 0027414922 scopus 로고
    • The baculovirus Autographa californica encodes a protein tyrosine phosphatase
    • Z Sheng H Charbonneau The baculovirus Autographa californica encodes a protein tyrosine phosphatase J. Biol. Chem. 268 1993 4728 4733
    • (1993) J. Biol. Chem. , vol.268 , pp. 4728-4733
    • Sheng, Z1    Charbonneau, H2
  • 78
    • 0031773604 scopus 로고    scopus 로고
    • Guanylyltransferase activity of the LEF-4 subunit of baculovirus RNA polymerase
    • L.A Guarino J Jin W Dong Guanylyltransferase activity of the LEF-4 subunit of baculovirus RNA polymerase J. Viral 72 1998 10003 10010
    • (1998) J. Viral , vol.72 , pp. 10003-10010
    • Guarino, L.A1    Jin, J2    Dong, W3
  • 79
    • 0029029529 scopus 로고
    • Properties of a baculovirus mutant defective in the protein phosphatase gene
    • Y Li L.K Miller Properties of a baculovirus mutant defective in the protein phosphatase gene J. Virol. 69 1995 4533 4537
    • (1995) J. Virol. , vol.69 , pp. 4533-4537
    • Li, Y1    Miller, L.K2
  • 80
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica nuclear polyhedrosis virus
    • M.D Avres S.C Howard J Kuzio M Lopez-Ferber R.D Possee The complete DNA sequence of Autographa californica nuclear polyhedrosis virus Virology 202 1994 586 605
    • (1994) Virology , vol.202 , pp. 586-605
    • Avres, M.D1    Howard, S.C2    Kuzio, J3    Lopez-Ferber, M4    Possee, R.D5
  • 81
    • 0032493642 scopus 로고    scopus 로고
    • PIR1 a novel phosphatase that exhibits high affinity to RNAribonucleoprotein complexes
    • Y Yuan D Li H Sun PIR1 a novel phosphatase that exhibits high affinity to RNAribonucleoprotein complexes J. Biol. Chem. 273 1998 20347 20353
    • (1998) J. Biol. Chem. , vol.273 , pp. 20347-20353
    • Yuan, Y1    Li, D2    Sun, H3
  • 82
    • 0030000857 scopus 로고    scopus 로고
    • Vaccinia virus mRNA (guanine-7-) methyltransferase: mutational effects on cap methylation and AdoHcy-dependent photocrosslinking of the cap to the methyl acceptor site
    • X Mao S Shuman Vaccinia virus mRNA (guanine-7-) methyltransferase: mutational effects on cap methylation and AdoHcy-dependent photocrosslinking of the cap to the methyl acceptor site Biochemistry 35 1996 6900 6910
    • (1996) Biochemistry , vol.35 , pp. 6900-6910
    • Mao, X1    Shuman, S2
  • 83
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse Sadenosylmethionine-dependent methyltransferases suggest a common structure for these enzymes
    • R.M Kagan S Clarke Widespread occurrence of three sequence motifs in diverse Sadenosylmethionine-dependent methyltransferases suggest a common structure for these enzymes Arch. Biochem. Biophys. 310 1994 417 427
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M1    Clarke, S2
  • 84
    • 0033534476 scopus 로고    scopus 로고
    • S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae
    • A Niewmierzycka S Clarke S -Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae J. Biol. Chem. 274 1999 814 824
    • (1999) J. Biol. Chem. , vol.274 , pp. 814-824
    • Niewmierzycka, A1    Clarke, S2
  • 85
    • 0029559311 scopus 로고
    • Sequence similarity of Escherichia coli proteins: functional and evolutionary implications
    • E.V Koonin R.L Tatusov K.E Rudd Sequence similarity of Escherichia coli proteins: functional and evolutionary implications 6th ed. Proc. Natl. Acad. Sci. USA 92 1995 11921 11925
    • (1995) , pp. 11921-11925
    • Koonin, E.V1    Tatusov, R.L2    Rudd, K.E3
  • 87
    • 85119551072 scopus 로고    scopus 로고
    • mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains
    • G Hu P.D Gershon A.E Hodel F.A Quiocho mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains 6th ed. Proc. Natl. Acad. Sci. USA 96 1999 49 54
    • (1999) , pp. 49-54
    • Hu, G1    Gershon, P.D2    Hodel, A.E3    Quiocho, F.A4
  • 88
    • 0031993338 scopus 로고    scopus 로고
    • Structural basis for sequence-nonspecific recognition of 5′-capped mRNA by a cap-modifying enzyme
    • A.E Hodel P.D Gershon F.A Quiocho Structural basis for sequence-nonspecific recognition of 5′-capped mRNA by a cap-modifying enzyme Mol. Cell. 1 1998 443 447
    • (1998) Mol. Cell. , vol.1 , pp. 443-447
    • Hodel, A.E1    Gershon, P.D2    Quiocho, F.A3
  • 89
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • J Marcotrigiano A Gingras N Sonenberg S.K Burley Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP Cell 89 1997 951 961
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J1    Gingras, A2    Sonenberg, N3    Burley, S.K4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.