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Volumn 26, Issue 23, 2007, Pages 4913-4925

Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase

Author keywords

Methyl transferase; mRNA capping enzyme; Poxvirus; S adenosyl homocysteine; X ray crystallography

Indexed keywords

MESSENGER RNA; METHYLTRANSFERASE; RNA; S ADENOSYLHOMOCYSTEINE;

EID: 36549088581     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601912     Document Type: Article
Times cited : (64)

References (52)
  • 2
    • 27744474787 scopus 로고    scopus 로고
    • Smallpox vaccine: The good, the bad, and the ugly
    • Belongia EA, Naleway AL (2003) Smallpox vaccine: the good, the bad, and the ugly. Clin Med Res 1: 87-92
    • (2003) Clin Med Res , vol.1 , pp. 87-92
    • Belongia, E.A.1    Naleway, A.L.2
  • 3
    • 0025861668 scopus 로고
    • A temperature-sensitive lesion in the small subunit of the vaccinia virus-encoded mRNA capping enzyme causes a defect in viral telomere resolution
    • Carpenter MS, DeLange AM (1991) A temperature-sensitive lesion in the small subunit of the vaccinia virus-encoded mRNA capping enzyme causes a defect in viral telomere resolution. J Virol 65: 4042-4050
    • (1991) J Virol , vol.65 , pp. 4042-4050
    • Carpenter, M.S.1    DeLange, A.M.2
  • 4
    • 0031453408 scopus 로고    scopus 로고
    • mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Cho EJ, Takagi T, Moore CR, Buratowski S (1997) mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev 11: 3319-3326
    • (1997) Genes Dev , vol.11 , pp. 3319-3326
    • Cho, E.J.1    Takagi, T.2    Moore, C.R.3    Buratowski, S.4
  • 5
    • 0026759583 scopus 로고
    • Methyltransferase and subunit association domains of vaccinia virus mRNA capping enzyme
    • Cong P, Shuman S (1992) Methyltransferase and subunit association domains of vaccinia virus mRNA capping enzyme. J Biol Chem 267: 16424-16429
    • (1992) J Biol Chem , vol.267 , pp. 16424-16429
    • Cong, P.1    Shuman, S.2
  • 8
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: Crystal structure and functional characterization
    • Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B (2002) An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J 21: 2757-2768
    • (2002) EMBO J , vol.21 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3    Romette, J.L.4    Canard, B.5
  • 9
    • 34548148632 scopus 로고    scopus 로고
    • Structural and functional analysis of methylation and 5′-RNA sequence requirements of short capped RNAs by the methyltransferase domain of dengue virus NS5
    • Egloff MP, Decroly E, Malet H, Selisko B, Benarroch D, Ferron F, Canard B (2007) Structural and functional analysis of methylation and 5′-RNA sequence requirements of short capped RNAs by the methyltransferase domain of dengue virus NS5. J Mol Biol 372: 723-736
    • (2007) J Mol Biol , vol.372 , pp. 723-736
    • Egloff, M.P.1    Decroly, E.2    Malet, H.3    Selisko, B.4    Benarroch, D.5    Ferron, F.6    Canard, B.7
  • 11
    • 1642482865 scopus 로고    scopus 로고
    • Structure and mechanism of mRNA cap (guanine-N7) methyltransferase
    • Fabrega C, Hausmann S, Shen V, Shuman S, Lima CD (2004) Structure and mechanism of mRNA cap (guanine-N7) methyltransferase. Mol Cell 13: 77-89
    • (2004) Mol Cell , vol.13 , pp. 77-89
    • Fabrega, C.1    Hausmann, S.2    Shen, V.3    Shuman, S.4    Lima, C.D.5
  • 12
    • 0038094496 scopus 로고    scopus 로고
    • Structure of an mRNA capping enzyme bound to the phosphorylated carboxyterminal domain of RNA polymerase II
    • Fabrega C, Shen V, Shuman S, Lima CD (2003) Structure of an mRNA capping enzyme bound to the phosphorylated carboxyterminal domain of RNA polymerase II. Mol Cell 11: 1549-1561
    • (2003) Mol Cell , vol.11 , pp. 1549-1561
    • Fabrega, C.1    Shen, V.2    Shuman, S.3    Lima, C.D.4
  • 13
    • 0026707685 scopus 로고
    • The vaccinia virus mRNA (guanine-N7-)-methyltransferase requires both subunits of the mRNA capping enzyme for activity
    • Higman MA, Bourgeois N, Niles EG (1992) The vaccinia virus mRNA (guanine-N7-)-methyltransferase requires both subunits of the mRNA capping enzyme for activity. J Biol Chem 267: 16430-16437
    • (1992) J Biol Chem , vol.267 , pp. 16430-16437
    • Higman, M.A.1    Bourgeois, N.2    Niles, E.G.3
  • 14
    • 0028239360 scopus 로고
    • The mRNA (guanine-7-) methyltransferase domain of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli and structural and kinetic comparison to the intact capping enzyme
    • Higman MA, Christen LA, Niles EG (1994) The mRNA (guanine-7-) methyltransferase domain of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli and structural and kinetic comparison to the intact capping enzyme. J Biol Chem 269: 14974-14981
    • (1994) J Biol Chem , vol.269 , pp. 14974-14981
    • Higman, M.A.1    Christen, L.A.2    Niles, E.G.3
  • 15
    • 0028362399 scopus 로고
    • Location of the S-adenosyl-L- methionine binding region of the vaccinia virus mRNA (guanine-7-) methyltransferase
    • Higman MA, Niles EG (1994) Location of the S-adenosyl-L- methionine binding region of the vaccinia virus mRNA (guanine-7-) methyltransferase. J Biol Chem 269: 14982-14987
    • (1994) J Biol Chem , vol.269 , pp. 14982-14987
    • Higman, M.A.1    Niles, E.G.2
  • 16
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233: 123-138
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 17
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26: 795-800
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 18
    • 0023693102 scopus 로고
    • Rat liver glycine methyltransferase. Cooperative binding of S-adenosylmethionine and loss of cooperativity by removal of a short NH 2-terminal segment
    • Konishi K, Fujioka M (1988) Rat liver glycine methyltransferase. Cooperative binding of S-adenosylmethionine and loss of cooperativity by removal of a short NH 2-terminal segment. J Biol Chem 263: 13381-13385
    • (1988) J Biol Chem , vol.263 , pp. 13381-13385
    • Konishi, K.1    Fujioka, M.2
  • 19
    • 1842505374 scopus 로고    scopus 로고
    • Zoonotic poxvirus infections in humans
    • Lewis-Jones S (2004) Zoonotic poxvirus infections in humans. Curr Opin Infect Dis 17: 81-89
    • (2004) Curr Opin Infect Dis , vol.17 , pp. 81-89
    • Lewis-Jones, S.1
  • 20
    • 0037441653 scopus 로고    scopus 로고
    • Lovell SC, Davis IW, Arendall III WB, de Bakker PI, Word JM, Prisant MG, Richardson JS, Richardson DC (2003) Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins 50: 437-450
    • Lovell SC, Davis IW, Arendall III WB, de Bakker PI, Word JM, Prisant MG, Richardson JS, Richardson DC (2003) Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins 50: 437-450
  • 22
    • 0028088458 scopus 로고
    • Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia virus capping enzyme D1 subunit is stimulated by the D12 subunit. Identification of amino acid residues in the D1 protein required for subunit association and methyl group transfer
    • Mao X, Shuman S (1994) Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia virus capping enzyme D1 subunit is stimulated by the D12 subunit. Identification of amino acid residues in the D1 protein required for subunit association and methyl group transfer. J Biol Chem 269: 24472-24479
    • (1994) J Biol Chem , vol.269 , pp. 24472-24479
    • Mao, X.1    Shuman, S.2
  • 23
    • 0030000857 scopus 로고    scopus 로고
    • Vaccinia virus mRNA (guanine-7-)methyltransferase: Mutational effects on cap methylation and AdoHcy-dependent photo-cross-linking of the cap to the methyl acceptor site
    • Mao X, Shuman S (1996) Vaccinia virus mRNA (guanine-7-)methyltransferase: mutational effects on cap methylation and AdoHcy-dependent photo-cross-linking of the cap to the methyl acceptor site. Biochemistry 35: 6900-6910
    • (1996) Biochemistry , vol.35 , pp. 6900-6910
    • Mao, X.1    Shuman, S.2
  • 24
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin JL, McMillan FM (2002) SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol 12: 783-793
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53: 240-255
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 27
    • 0030007647 scopus 로고    scopus 로고
    • Characterization of the vaccinia virus RNA 5′-triphosphatase and nucleotide triphosphate phosphohydrolase activities. Demonstrate that both activities are carried out at the same active site
    • Myette JR, Niles EG (1996) Characterization of the vaccinia virus RNA 5′-triphosphatase and nucleotide triphosphate phosphohydrolase activities. Demonstrate that both activities are carried out at the same active site. J Biol Chem 271: 11945-11952
    • (1996) J Biol Chem , vol.271 , pp. 11945-11952
    • Myette, J.R.1    Niles, E.G.2
  • 28
    • 0027424399 scopus 로고
    • Identification of the vaccinia virus mRNA guanyltransferase active site lysine
    • Niles EG, Christen L (1993) Identification of the vaccinia virus mRNA guanyltransferase active site lysine. J Biol Chem 268: 24986-24989
    • (1993) J Biol Chem , vol.268 , pp. 24986-24989
    • Niles, E.G.1    Christen, L.2
  • 29
    • 4544339401 scopus 로고    scopus 로고
    • Glycine N-methyltransferases: A comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes
    • Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME (2004) Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes. Proteins 57: 331-337
    • (2004) Proteins , vol.57 , pp. 331-337
    • Pakhomova, S.1    Luka, Z.2    Grohmann, S.3    Wagner, C.4    Newcomer, M.E.5
  • 30
    • 33748669852 scopus 로고    scopus 로고
    • West Nile virus 5′-cap structure is formed by sequential guanine N-7 and ribose 2′-O methylations by nonstructural protein 5
    • Ray D, Shah A, Tilgner M, Guo Y, Zhao Y, Dong H, Deas TS, Zhou Y, Li H, Shi PY (2006) West Nile virus 5′-cap structure is formed by sequential guanine N-7 and ribose 2′-O methylations by nonstructural protein 5. J Virol 80: 8362-8370
    • (2006) J Virol , vol.80 , pp. 8362-8370
    • Ray, D.1    Shah, A.2    Tilgner, M.3    Guo, Y.4    Zhao, Y.5    Dong, H.6    Deas, T.S.7    Zhou, Y.8    Li, H.9    Shi, P.Y.10
  • 31
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6Å resolution
    • Reinisch KM, Nibert ML, Harrison SC (2000) Structure of the reovirus core at 3.6Å resolution. Nature 404: 960-967
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 32
    • 0035881512 scopus 로고    scopus 로고
    • Effects of alanine cluster mutations in the D12 subunit of vaccinia virus mRNA (guanine-N7) methyltransferase
    • Saha N, Shuman S (2001) Effects of alanine cluster mutations in the D12 subunit of vaccinia virus mRNA (guanine-N7) methyltransferase. Virology 287: 40-48
    • (2001) Virology , vol.287 , pp. 40-48
    • Saha, N.1    Shuman, S.2
  • 33
    • 0038339628 scopus 로고    scopus 로고
    • Yeast-based genetic system for functional analysis of poxvirus mRNA cap methyltransferase
    • Saha N, Shuman S, Schwer B (2003) Yeast-based genetic system for functional analysis of poxvirus mRNA cap methyltransferase. J Virol 77: 7300-7307
    • (2003) J Virol , vol.77 , pp. 7300-7307
    • Saha, N.1    Shuman, S.2    Schwer, B.3
  • 34
    • 4644275047 scopus 로고    scopus 로고
    • Consequences of binding an S-adenosylmethionine analogue on the structure and dynamics of the thiopurine methyltransferase protein backbone
    • Scheuermann TH, Keeler C, Hodsdon ME (2004) Consequences of binding an S-adenosylmethionine analogue on the structure and dynamics of the thiopurine methyltransferase protein backbone. Biochemistry 43: 12198-12209
    • (2004) Biochemistry , vol.43 , pp. 12198-12209
    • Scheuermann, T.H.1    Keeler, C.2    Hodsdon, M.E.3
  • 35
    • 0026522879 scopus 로고
    • Cap-specific mRNA (nucleoside-O2′-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein
    • Schnierle BS, Gershon PD, Moss B (1992) Cap-specific mRNA (nucleoside-O2′-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein. Proc Natl Acad Sci USA 89: 2897-2901
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2897-2901
    • Schnierle, B.S.1    Gershon, P.D.2    Moss, B.3
  • 36
    • 33745868309 scopus 로고    scopus 로고
    • Poxvirus mRNA cap methyltransferase. Bypass of the requirement for the stimulatory subunit by mutations in the catalytic subunit and evidence for intersubunit allostery
    • Schwer B, Hausmann S, Schneider S, Shuman S (2006) Poxvirus mRNA cap methyltransferase. Bypass of the requirement for the stimulatory subunit by mutations in the catalytic subunit and evidence for intersubunit allostery. J Biol Chem 281: 18953-18960
    • (2006) J Biol Chem , vol.281 , pp. 18953-18960
    • Schwer, B.1    Hausmann, S.2    Schneider, S.3    Shuman, S.4
  • 37
    • 33746518147 scopus 로고    scopus 로고
    • Genetic analysis of poxvirus mRNA cap methyltransferase: Suppression of conditional mutations in the stimulatory D12 subunit by second-site mutations in the catalytic D1 subunit
    • Schwer B, Shuman S (2006) Genetic analysis of poxvirus mRNA cap methyltransferase: suppression of conditional mutations in the stimulatory D12 subunit by second-site mutations in the catalytic D1 subunit. Virology 352: 145-156
    • (2006) Virology , vol.352 , pp. 145-156
    • Schwer, B.1    Shuman, S.2
  • 38
    • 0024383396 scopus 로고
    • Functional domains of vaccinia virus mRNA capping enzyme. Analysis by limited tryptic digestion
    • Shuman S (1989) Functional domains of vaccinia virus mRNA capping enzyme. Analysis by limited tryptic digestion. J Biol Chem 264: 9690-9695
    • (1989) J Biol Chem , vol.264 , pp. 9690-9695
    • Shuman, S.1
  • 39
    • 0035201941 scopus 로고    scopus 로고
    • Structure, mechanism, and evolution of the mRNA capping apparatus
    • Shuman S (2001) Structure, mechanism, and evolution of the mRNA capping apparatus. Prog Nucleic Acid Res Mol Biol 66: 1-40
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.66 , pp. 1-40
    • Shuman, S.1
  • 40
    • 0036347305 scopus 로고    scopus 로고
    • What messenger RNA capping tells us about eukaryotic evolution
    • Shuman S (2002) What messenger RNA capping tells us about eukaryotic evolution. Nat Rev Mol Cell Biol 3: 619-625
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 619-625
    • Shuman, S.1
  • 41
    • 0023917984 scopus 로고
    • Factor-dependent transcription termination by vaccinia virus RNA polymerase. Evidence that the cisacting termination signal is in nascent RNA
    • Shuman S, Moss B (1988) Factor-dependent transcription termination by vaccinia virus RNA polymerase. Evidence that the cisacting termination signal is in nascent RNA. J Biol Chem 263: 6220-6225
    • (1988) J Biol Chem , vol.263 , pp. 6220-6225
    • Shuman, S.1    Moss, B.2
  • 42
    • 0019205794 scopus 로고
    • Purification and characterization of a GTP-pyrophosphate exchange activity from vaccinia virions. Association of the GTP-pyrophosphate exchange activity with vaccinia mRNA guanylyltransferase. RNA (guanine-7-)methyltransferase complex (capping enzyme)
    • Shuman S, Surks M, Furneaux H, Hurwitz J (1980) Purification and characterization of a GTP-pyrophosphate exchange activity from vaccinia virions. Association of the GTP-pyrophosphate exchange activity with vaccinia mRNA guanylyltransferase. RNA (guanine-7-)methyltransferase complex (capping enzyme). J Biol Chem 255: 11588-11598
    • (1980) J Biol Chem , vol.255 , pp. 11588-11598
    • Shuman, S.1    Surks, M.2    Furneaux, H.3    Hurwitz, J.4
  • 43
    • 0036635507 scopus 로고    scopus 로고
    • Smallpox: Anything to declare?
    • Smith GL, McFadden G (2002) Smallpox: anything to declare? Nat Rev Immunol 2: 521-527
    • (2002) Nat Rev Immunol , vol.2 , pp. 521-527
    • Smith, G.L.1    McFadden, G.2
  • 47
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification, and model building
    • Terwilliger T (2004) SOLVE and RESOLVE: automated structure solution, density modification, and model building. J Synchrotron Radiat 11: 49-52
    • (2004) J Synchrotron Radiat , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 48
    • 35348916034 scopus 로고    scopus 로고
    • Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains
    • Troffer-Charlier N, Cura V, Hassenboehler P, Moras D, Cavarelli J (2007) Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains. EMBO J 26: 4391-4401
    • (2007) EMBO J , vol.26 , pp. 4391-4401
    • Troffer-Charlier, N.1    Cura, V.2    Hassenboehler, P.3    Moras, D.4    Cavarelli, J.5
  • 49
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography
    • Uson I, Sheldrick GM (1999) Advances in direct methods for protein crystallography. Curr Opin Struct Biol 9: 643-648
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 643-648
    • Uson, I.1    Sheldrick, G.M.2
  • 50
    • 0025783910 scopus 로고
    • Vaccinia virus capping enzyme is a transcription initiation factor
    • Vos JC, Sasker M, Stunnenberg HG (1991) Vaccinia virus capping enzyme is a transcription initiation factor. EMBO J 10: 2553-2558
    • (1991) EMBO J , vol.10 , pp. 2553-2558
    • Vos, J.C.1    Sasker, M.2    Stunnenberg, H.G.3
  • 51
    • 35348861410 scopus 로고    scopus 로고
    • Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase
    • Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH (2007) Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase. EMBO J 26: 4402-4412
    • (2007) EMBO J , vol.26 , pp. 4402-4412
    • Yue, W.W.1    Hassler, M.2    Roe, S.M.3    Thompson-Vale, V.4    Pearl, L.H.5


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