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Volumn 211, Issue 1, 1995, Pages 73-83

Mutational analysis of vaccinia DNA ligase defines residues essential for covalent catalysis

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EID: 0029152217     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1995.1380     Document Type: Article
Times cited : (56)

References (40)
  • 1
    • 0023019231 scopus 로고
    • Different substrate specificities of the two DNA ligases of mammalian cells
    • t Willis, A. E., Goldsmith, I., and Lindahl, T. (1986). Different substrate specificities of the two DNA ligases of mammalian cells. J. Biol. Chem. 261, 9079-9082.
    • (1986) J. Biol. Chem , vol.261 , pp. 9079-9082
    • Arrand Willis, J.E.A.E.1    Goldsmith, I.2    Lindahl, T.3
  • 2
    • 0022422374 scopus 로고
    • The nucleotide sequence of the DNA ligase gene (CDC9) from Saccharomyces cere-visiae: A gene which is cell cycle regulated and induced in response to DNA damage
    • Barker, D. G., White, J., and Johnston, L H. (1985). The nucleotide sequence of the DNA ligase gene (CDC9) from Saccharomyces cere-visiae: A gene which is cell cycle regulated and induced in response to DNA damage. Nucleic Acids Res. 13, 8323-8337.
    • (1985) Nucleic Acids Res , vol.13 , pp. 8323-8337
    • Barker, D.G.1    White, J.2    Johnston, L.H.3
  • 3
    • 0023118309 scopus 로고
    • Molecular characterization of the DNA ligase gene, CDC17, from the fission yeast Schiz-osaccharomyces pombe. Eur
    • Barker, D. G, White, J., and Johnston, L. H. (1987). Molecular characterization of the DNA ligase gene, CDC17, from the fission yeast Schiz-osaccharomyces pombe. Eur. J. Biochem. 162, 659-667.
    • (1987) J. Biochem , vol.162 , pp. 659-667
    • Barker, D.G.1    White, J.2    Johnston, L.H.3
  • 5
    • 0025091655 scopus 로고
    • A DNA ligase gene in the Copenhagen strain of vaccinia virus is nonessential for viral replication and recombination
    • Colinas, R. J., Goebel, S. J., Davis, S. W, Johnson, G. P., Norton, E. «., and Paoletti, E. (1990). A DNA ligase gene in the Copenhagen strain of vaccinia virus is nonessential for viral replication and recombination. Virology 179, 267-275.
    • (1990) Virology , vol.179 , pp. 267-275
    • Colinas, R.J.1    Goebel, S.J.2    Davis, S.W.3    Johnson, G.P.4    Norton, E.5    Paoletti, E.6
  • 6
    • 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
    • Cong, P., and Shuman, S. (1993). 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, 7256-7260.
    • (1993) J. Biol. Chem , vol.268 , pp. 7256-7260
    • Cong, P.1    Shuman, S.2
  • 8
    • 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
    • Fresco, L. D., and Buratowski, S. (1994). Active site of the mRNA capping enzyme guanylyltransferase from Saccharomyces cerevisiae: Similarity to the nucleotidyl attachment motif of DNA and RNA ligases, Proc. Natl. Acad. Sci. USA 91, 6624-6628.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6624-6628
    • Fresco, L.D.1    Buratowski, S.2
  • 9
    • 0026778242 scopus 로고
    • An African swine fever virus gene with homology to DNA ligases
    • Hammond, J. M., Kerr, S. M., Smith, G. L, and Dixon, L. K. (1992). An African swine fever virus gene with homology to DNA ligases. Nucleic Acids Res. 20, 2667-2671.
    • (1992) Nucleic Acids Res , vol.20 , pp. 2667-2671
    • Hammond, J.M.1    Kerr, S.M.2    Smith, G.L.3    Dixon, L.K.4
  • 10
    • 0023663357 scopus 로고
    • Effect of single amino acid changes in the region of the adenylylation site ofT4 RNA ligase
    • Heaphy, S., Singh, M., and Gait, M. J. (1987). Effect of single amino acid changes in the region of the adenylylation site ofT4 RNA ligase. Biochemistry 26, 1688-1696.
    • (1987) Biochemistry , vol.26
    • Heaphy, S.1    Singh, M.2    Gait, M.J.3
  • 11
    • 0016808563 scopus 로고
    • Bacteriophage T7 deoxyribonucleic acid replication in vitro: Purification and properties of the gene 4 protein of bacteriophage T7
    • Hinkle, D. C., and Richardson, C. C. (1975). Bacteriophage T7 deoxyribonucleic acid replication in vitro: Purification and properties of the gene 4 protein of bacteriophage T7. J. Biol. Chem. 250, 5523-5529.
    • (1975) J. Biol. Chem , vol.250 , pp. 5523-5529
    • Hinkle, D.C.1    Richardson, C.C.2
  • 12
    • 0024329572 scopus 로고
    • Vaccinia virus encodes a polypeptide with DNA ligase activity
    • Kerr, S. M„ and Smith, G. L. (1989). Vaccinia virus encodes a polypeptide with DNA ligase activity. Nucleic Acids Res. 17, 9039-9050.
    • (1989) Nucleic Acids Res , vol.17 , pp. 9039-9050
    • Kerr, S.M.1    Smith, G.L.2
  • 13
    • 0026061401 scopus 로고
    • Vaccinia DNA ligase complements Saccharomyces cerevisiae cdc9, localizes in cytoplasmic factories and affects virulence and virus sensitivity to DNA damaging agents
    • Kerr, S. M., Johnston, L. H., Odell, M., Duncan, S. A., Law, K. M., and Smith, G, L. (1991). Vaccinia DNA ligase complements Saccharomyces cerevisiae cdc9, localizes in cytoplasmic factories and affects virulence and virus sensitivity to DNA damaging agents. EMBO J. 10, 4343-4350.
    • (1991) EMBO J , vol.10 , pp. 4343-4350
    • Kerr, S.M.1    Johnston, L.H.2    Odell, M.3    Duncan, S.A.4    Law, K.M.5    Smith, G.6
  • 14
    • 0026017350 scopus 로고
    • Vaccinia virus DNA ligase is nonessential for virus replication: Recovery of plasmids from virus-infected cells
    • Kerr, S. M., and Smith, G. L. (1991). Vaccinia virus DNA ligase is nonessential for virus replication: Recovery of plasmids from virus-infected cells. Virology 180, 625-632.
    • (1991) Virology , vol.180 , pp. 625-632
    • Kerr, S.M.1    Smith, G.L.2
  • 15
    • 0026661136 scopus 로고
    • Molecular characterization of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogentic relationship to eukaryotic ligases
    • Kletzin, A. (1992). Molecular characterization of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogentic relationship to eukaryotic ligases. Nucleic Acids Res. 20, 5389-5396.
    • (1992) Nucleic Acids Res , vol.20 , pp. 5389-5396
    • Kletzin, A.1
  • 16
    • 0026059034 scopus 로고
    • In vitro mutagenesis and functional expression in Escherichia coii of a cDNA encoding the catalytic domain of human DNA ligase I
    • Kodama, K., Barnes, D. E., and Lindahl, T. (1991). In vitro mutagenesis and functional expression in Escherichia coii of a cDNA encoding the catalytic domain of human DNA ligase I. Nucleic Acids Res. 19, 6093-6099.
    • (1991) Nucleic Acids Res , vol.19 , pp. 6093-6099
    • Kodama, K.1    Barnes, D.E.2    Lindahl, T.3
  • 17
    • 0016273515 scopus 로고
    • DNA ligase: Structure, mechanism, and function
    • Lehman, I. R. (1974). DNA ligase: Structure, mechanism, and function. Science 186, 790-797.
    • (1974) Science , vol.186 , pp. 790-797
    • Lehman, I.R.1
  • 18
    • 0026693965 scopus 로고
    • Mammalian DNA ligases, Annu
    • Lindahl, T., and Barnes, D. E. (1992). Mammalian DNA ligases, Annu. Rev. Biochem. 61, 251-281
    • (1992) Rev. Biochem , vol.61 , pp. 251-281
    • Lindahl, T.1    Barnes, D.E.2
  • 19
    • 0025043782 scopus 로고
    • Use of ATP, dATP and their cr-thio derivatives to study ligase adenylation
    • Montecucco, A, Lestingi, M., Pedrali-Noy, G., Spadari, S., and Ciaroc-chi, G. (1990). Use of ATP, dATP and their cr-thio derivatives to study ligase adenylation. Biochem. J. 271, 265-268.
    • (1990) Biochem. J , vol.271 , pp. 265-268
    • Montecucco, A.1    Lestingi, M.2    Pedrali-Noy, G.3    Spadari, S.4    Ciaroc-Chi, G.5
  • 20
    • 0027424399 scopus 로고
    • Identification of the vaccinia virus mRNA guanylyitransferase active site lysine
    • Niles, E. G., and Christen, L. (1993). Identification of the vaccinia virus mRNA guanylyitransferase 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
  • 21
    • 0027993607 scopus 로고
    • Characterization of the Shope fibroma virus DNA ligase gene
    • Parks, R. J., Lichty, B. D., Karakis, C., and Evans, D. H. (1994). Characterization of the Shope fibroma virus DNA ligase gene. Virology 202, 642-650.
    • (1994) Virology , vol.202 , pp. 642-650
    • Parks, R.J.1    Lichty, B.D.2    Karakis, C.3    Evans, D.H.4
  • 22
    • 0027312425 scopus 로고
    • African swine fever virus guanylyitransferase
    • Pena, L, Yanez, R., Revilla, Y„ Vinuela, E., and Salas, M. L. (1992), African swine fever virus guanylyitransferase. Virology 193, 319-328.
    • (1992) Virology , vol.193 , pp. 319-328
    • Pena, L.1    Yanez, R.2    Revilla Vinuela, Y.E.3    Salas, M.L.4
  • 23
    • 0021377916 scopus 로고
    • Sequence and cioning of bacteriophage T4 gene 63 encoding RNA ligase and tail fibre attachment activities
    • Rand, K. N., and Gait, M. J. (1984). Sequence and cioning of bacteriophage T4 gene 63 encoding RNA ligase and tail fibre attachment activities. EMBO J. 3, 397-402.
    • (1984) EMBO J , vol.3 , pp. 397-402
    • Rand, K.N.1    Gait, M.J.2
  • 24
    • 0028211258 scopus 로고
    • Mutational analysis of yeast mRNA capping enzyme
    • Schwer, B., and Shuman, S. (1994). Mutational analysis of yeast mRNA capping enzyme. Proc. Natl. Acad. Set. USA 91, 4328-4332.
    • (1994) Proc. Natl. Acad. Set. USA , vol.91 , pp. 4328-4332
    • Schwer, B.1    Shuman, S.2
  • 25
    • 0026733001 scopus 로고
    • MRNA capping enzyme: Isolation and characterization of the gene encoding mRNA guanylyitransferase subunit from Saccharomyces cerevisiae
    • Shibagaki, Y., Itoh, N„ Yamada, H., Nagata, S., and Mizumoto, K. (1992). mRNA capping enzyme: isolation and characterization of the gene encoding mRNA guanylyitransferase subunit from Saccharomyces cerevisiae. J. Biol. Chem. 267, 9521-9528.
    • (1992) J. Biol. Chem , vol.267 , pp. 9521-9528
    • Shibagaki, Y.1    Itoh, N.2    Yamada, H.3    Nagata, S.4    Mizumoto, K.5
  • 26
    • 0029107231 scopus 로고
    • Capping enzyme in eukaryotic mRNA synthesis
    • Shuman, S. (1995). Capping enzyme in eukaryotic mRNA synthesis. Prog. Nucleic Acid Res. Moi. Biol. 50, 101-129.
    • (1995) Prog. Nucleic Acid Res. Moi. Biol , vol.50 , pp. 101-129
    • Shuman, S.1
  • 27
    • 0000262312 scopus 로고
    • Mechanism of mRNA capping by vaccinia virus guanylyitransferase: Characterization of an enzyme-guanylate intermediate
    • Shuman, S., and Hurwitz, J. (1981). Mechanism of mRNA capping by vaccinia virus guanylyitransferase: Characterization of an enzyme-guanylate intermediate. Proc. Natl. Acad. Sci. USA 78, 187-191.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 187-191
    • Shuman, S.1    Hurwitz, J.2
  • 28
    • 0028172876 scopus 로고
    • Covalent catalysis in nucleo-tidy transfer reactions: Essential motifs in Saccharomyces cerevisiae capping enzyme are conserved in Schizosaccharomycespombe and viral capping enzymes and among polynucleotide ligases
    • Shuman, S., Liu, Y., and Schwer, B. (1994). Covalent catalysis in nucleo-tidy transfer reactions: Essential motifs in Saccharomyces cerevisiae capping enzyme are conserved in Schizosaccharomycespombe and viral capping enzymes and among polynucleotide ligases. Proc. Natl. Acad. Sci. USA 91, 12046-12050.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12046-12050
    • Shuman, S.1    Liu, Y.2    Schwer, B.3
  • 29
    • 0028058938 scopus 로고
    • Deletion of fowlpox virus homologues of vaccinia genes between the 3/J-hydroxysteroid dehydrogenase (A44L) and DNA ligase (A50R) genes
    • Skinner, M. A., Moore, J. B., Binns, M. M., Smith, G. L, and Boursnell, M. E. G. (1994). Deletion of fowlpox virus homologues of vaccinia genes between the 3/J-hydroxysteroid dehydrogenase (A44L) and DNA ligase (A50R) genes. J. Gen. Virol. 75, 2495-2498.
    • (1994) J. Gen. Virol , vol.75 , pp. 2495-2498
    • Skinner, M.A.1    Moore, J.B.2    Binns, M.M.3    Smith, G.L.4    Boursnell, M.E.G.5
  • 30
    • 0024377646 scopus 로고
    • Transcriptional mapping and nucleotide sequence of a vaccinia gene encoding a polypeptide with extensive homology to DNA ligases
    • Smith, G. L., Chan, Y. S., and Kerr, S. M. (1989). Transcriptional mapping and nucleotide sequence of a vaccinia gene encoding a polypeptide with extensive homology to DNA ligases. Nucleic Acids Res. 17, 9051-9062.
    • (1989) Nucleic Acids Res , vol.17 , pp. 9051-9062
    • Smith, G.L.1    Chan, Y.S.2    Kerr, S.M.3
  • 31
  • 33
    • 0026011091 scopus 로고
    • Location of the active site for enzyme-adenylate formation in DNA ligases
    • Tomkinson, A. E., Totty, N. F., Ginsburg, M., and Lindahl, T. (1991b). Location of the active site for enzyme-adenylate formation in DNA ligases. Proc. Nati. Acad. Sci. USA 88, 400-404.
    • (1991) Proc. Nati. Acad. Sci. USA , vol.88 , pp. 400-404
    • Tomkinson, A.E.1    Totty, N.F.2    Ginsburg, M.3    Lindahl, T.4
  • 35
    • 0025769407 scopus 로고
    • Identification and DNA sequence of the large subunit of the capping enzyme from Shope fibroma virus
    • Upton, C., Stuart, D., and McFadden, G. (1991). Identification and DNA sequence of the large subunit of the capping enzyme from Shope fibroma virus. Virology 183, 773-777.
    • (1991) Virology , vol.183 , pp. 773-777
    • Upton, C.1    Stuart, D.2    McFadden, G.3
  • 38
    • 0023834872 scopus 로고
    • Structure and function of the yeast tRNA ligase gene
    • Westaway, S. K., Phizicky, E. M., and Abelson, J. (1988). Structure and function of the yeast tRNA ligase gene. J. Biol. Chem. 263, 3171-3176.
    • (1988) J. Biol. Chem , vol.263
    • Westaway, S.K.1    Phizicky, E.M.2    Abelson, J.3
  • 39
    • 0025296609 scopus 로고
    • Domain structure in yeast tRNA ligase
    • Xu, G., Teplow, D., Lee, T. D., and Abelson, J. (1990). Domain structure in yeast tRNA ligase. Biochemistry 29, 6132-6138.
    • (1990) Biochemistry , vol.29 , pp. 6132-6138
    • Xu, G.1    Teplow, D.2    Lee, T.D.3    Abelson, J.4
  • 40
    • 3042689834 scopus 로고
    • Macromolecular crowding allows blunt-end ligation by DNA ligases from rat liver or Escherichia coli
    • Zimmerman, S. B., and Pheiffer, B. H. (1983). Macromolecular crowding allows blunt-end ligation by DNA ligases from rat liver or Escherichia coli. Proc. Natl. Acad. Sci. USA 80, 5852-5856.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5852-5856
    • Zimmerman, S.B.1    Pheiffer, B.H.2


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