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Volumn 31, Issue 16, 2003, Pages 4950-4957

Characterisation of the substrate specificity of homogeneous vaccinia virus uracil-DNA glycosylase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSINE; ENZYME INHIBITOR; MAGNESIUM CHLORIDE; SMALLPOX VACCINE; URACIL; URACIL DNA GLYCOSYLTRANSFERASE; VIRUS ENZYME;

EID: 0345306586     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg672     Document Type: Article
Times cited : (35)

References (45)
  • 2
    • 0001142643 scopus 로고    scopus 로고
    • Poxviridae: The virus and their replication
    • Knipe,D.M. and Howley,P.M. (eds), Raven Press, New York
    • Moss,B. (2001) Poxviridae: the virus and their replication. In Knipe,D.M. and Howley,P.M. (eds), Fields Virology. Raven Press, New York, Vol. 2, pp. 2849-2884.
    • (2001) Fields Virology , vol.2 , pp. 2849-2884
    • Moss, B.1
  • 3
    • 0025079746 scopus 로고
    • Poxviruses: An emerging portrait of biological strategy
    • Traktman,P. (1990) Poxviruses: an emerging portrait of biological strategy. Cell, 62, 621-626.
    • (1990) Cell , vol.62 , pp. 621-626
    • Traktman, P.1
  • 5
    • 0000793742 scopus 로고    scopus 로고
    • Poxvirus DNA replication
    • DePamphilis,M.L. (ed.), Cold Spring Harbor Laboratory Press, New York
    • Traktman,P. (1996) Poxvirus DNA replication. In DePamphilis,M.L. (ed.), DNA Replication in Eucaryotic Cells. Cold Spring Harbor Laboratory Press, New York, pp. 775-793.
    • (1996) DNA Replication in Eucaryotic Cells , pp. 775-793
    • Traktman, P.1
  • 6
    • 0029976870 scopus 로고    scopus 로고
    • Genetically engineered poxviruses for recombinant gene expression, vaccination and safety
    • Moss,B. (1996) Genetically engineered poxviruses for recombinant gene expression, vaccination and safety. Proc. Natl Acad. Sci. USA, 93, 11341-11348.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11341-11348
    • Moss, B.1
  • 7
    • 0027418033 scopus 로고
    • A poxvirus-encoded uracil DNA glycosylase is essential for virus viability
    • Stuart,D.T., Upton,C., Higman,M.A., Niles,E.G. and McFadden,G. (1993) A poxvirus-encoded uracil DNA glycosylase is essential for virus viability. J. Virol., 67, 2503-2512.
    • (1993) J. Virol. , vol.67 , pp. 2503-2512
    • Stuart, D.T.1    Upton, C.2    Higman, M.A.3    Niles, E.G.4    McFadden, G.5
  • 8
    • 0028298871 scopus 로고
    • The vaccinia virus-encoded uracil DNA glycosylase has an essential role in viral DNA replication
    • Millns,A.K., Carpenter,M.S. and DeLange,A.M. (1994) The vaccinia virus-encoded uracil DNA glycosylase has an essential role in viral DNA replication. Virology, 198, 504-513.
    • (1994) Virology , vol.198 , pp. 504-513
    • Millns, A.K.1    Carpenter, M.S.2    DeLange, A.M.3
  • 9
    • 0027241184 scopus 로고
    • Identification of a poxvirus gene encoding a uracil DNA glycosylase
    • Upton,C., Stuart,D.T. and McFadden,G. (1993) Identification of a poxvirus gene encoding a uracil DNA glycosylase. Proc. Natl Acad. Sci. USA, 90, 4518-4522.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4518-4522
    • Upton, C.1    Stuart, D.T.2    McFadden, G.3
  • 10
    • 0025307073 scopus 로고
    • Nucleotide sequence analysis of a 10.5 kbp HindIII fragment of fowlpox virus: Relatedness to the central portion of the vaccinia virus HindIII D region
    • Tartaglia,J., Winslow,J., Goebel,S., Johnson,G.P., Taylor,J. and Paoletti,E. (1990) Nucleotide sequence analysis of a 10.5 kbp HindIII fragment of fowlpox virus: relatedness to the central portion of the vaccinia virus HindIII D region. J. Gen. Virol., 71, 1517-1524.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1517-1524
    • Tartaglia, J.1    Winslow, J.2    Goebel, S.3    Johnson, G.P.4    Taylor, J.5    Paoletti, E.6
  • 11
    • 0035225455 scopus 로고    scopus 로고
    • Keynote: Past, present and future aspects of base excision repair
    • Lindahl,T. (2001) Keynote: past, present and future aspects of base excision repair. Prog. Nucleic Acid Res. Mol. Biol., 68, xvii-xxx.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.68
    • Lindahl, T.1
  • 12
    • 0019483873 scopus 로고
    • Stimulation of the nuclear uracil DNA glycosylase in proliferating human fibroblasts
    • Gupta,P.K. and Sirover,M.A. (1981) Stimulation of the nuclear uracil DNA glycosylase in proliferating human fibroblasts. Cancer Res., 41, 3133-3136.
    • (1981) Cancer Res. , vol.41 , pp. 3133-3136
    • Gupta, P.K.1    Sirover, M.A.2
  • 14
    • 0016257644 scopus 로고
    • Heat-induced deamination of cytosine residues in deoxyribonucleic acid
    • Lindahl,T. and Nyberg,B. (1974) Heat-induced deamination of cytosine residues in deoxyribonucleic acid. Biochemistry, 13, 3405-3410.
    • (1974) Biochemistry , vol.13 , pp. 3405-3410
    • Lindahl, T.1    Nyberg, B.2
  • 15
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase beta and the XRCC1 protein
    • Kubota,Y., Nash,R.A., Klungland,A., Schar,P., Barnes,D.E. and Lindahl,T. (1996) Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. EMBO J., 15, 6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 16
    • 0024520122 scopus 로고
    • Gene UL2 of herpes simplex virus type 1 encodes a uracil-DNA glycosylase
    • Mullaney,J., Moss,H.W. and McGeoch,D.J. (1989) Gene UL2 of herpes simplex virus type 1 encodes a uracil-DNA glycosylase. J. Gen. Virol., 70, 449-454.
    • (1989) J. Gen. Virol. , vol.70 , pp. 449-454
    • Mullaney, J.1    Moss, H.W.2    McGeoch, D.J.3
  • 17
    • 0032567095 scopus 로고    scopus 로고
    • Expression of a uracil DNA glycosylase (UNG) inhibitor in mammalian cells: Varicella-zoster virus can replicate in vitro in the absence of detectable UNG activity
    • Reddy,S.M., Williams,M. and Cohen,J.I. (1998) Expression of a uracil DNA glycosylase (UNG) inhibitor in mammalian cells: varicella-zoster virus can replicate in vitro in the absence of detectable UNG activity. Virology, 251, 393-401.
    • (1998) Virology , vol.251 , pp. 393-401
    • Reddy, S.M.1    Williams, M.2    Cohen, J.I.3
  • 18
    • 0030971775 scopus 로고    scopus 로고
    • Construction of a vaccinia virus deficient in the essential DNA repair enzyme uracil DNA glycosylase by a complementing cell line
    • Holzer,G.W. and Falkner,F.G. (1997) Construction of a vaccinia virus deficient in the essential DNA repair enzyme uracil DNA glycosylase by a complementing cell line. J. Virol., 71, 4997-5002.
    • (1997) J. Virol. , vol.71 , pp. 4997-5002
    • Holzer, G.W.1    Falkner, F.G.2
  • 19
    • 0029845801 scopus 로고    scopus 로고
    • Mutations in active-site residues of the uracil-DNA glycosylase encoded by vaccinia virus are incompatible with virus viability
    • Ellison,K.S., Peng,W. and McFadden,G. (1996) Mutations in active-site residues of the uracil-DNA glycosylase encoded by vaccinia virus are incompatible with virus viability. J. Virol., 70, 7965-7973.
    • (1996) J. Virol. , vol.70 , pp. 7965-7973
    • Ellison, K.S.1    Peng, W.2    McFadden, G.3
  • 20
    • 0037213268 scopus 로고    scopus 로고
    • Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: Catalytic site mutations reduce virulence but not virus replication in cultured cells
    • De Silva,F.S. and Moss,B. (2003) Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: catalytic site mutations reduce virulence but not virus replication in cultured cells. J. Virol., 77, 159-166.
    • (2003) J. Virol. , vol.77 , pp. 159-166
    • De Silva, F.S.1    Moss, B.2
  • 21
    • 0028933306 scopus 로고
    • Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase
    • Slupphaug,G., Eftedal,I., Kavli,B., Bharati,S., Helle,N.M., Haug,T., Levine,D.W. and Krokan,H.E. (1995) Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase. Biochemistry, 34, 128-138.
    • (1995) Biochemistry , vol.34 , pp. 128-138
    • Slupphaug, G.1    Eftedal, I.2    Kavli, B.3    Bharati, S.4    Helle, N.M.5    Haug, T.6    Levine, D.W.7    Krokan, H.E.8
  • 22
    • 18644363009 scopus 로고    scopus 로고
    • hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches and U in single-stranded DNA, with hSMUG1 as a broad specificity backup
    • Kavli,B., Sundheim,O., Akbari,M., Otterlei,M., Nilsen,H., Skorpen,F., Aas,P.A., Hagen,L., Krokan,H.E. and Slupphaug,G. (2002) hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches and U in single-stranded DNA, with hSMUG1 as a broad specificity backup. J. Biol. Chem., 277, 39926-39936.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39926-39936
    • Kavli, B.1    Sundheim, O.2    Akbari, M.3    Otterlei, M.4    Nilsen, H.5    Skorpen, F.6    Aas, P.A.7    Hagen, L.8    Krokan, H.E.9    Slupphaug, G.10
  • 23
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • Slupphaug,G., Mol,C.D., Kavli,B., Arvai,A.S., Krokan,H.E. and Tainer,J.A. (1996) A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature, 384, 87-92.
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 24
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh,S.S., Mol,C.D., Slupphaug,G., Bharati,S., Krokan,H.E. and Tainer,J.A. (1998) Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J., 17, 5214-5226.
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 25
    • 0029084487 scopus 로고
    • Crystal structure of human uracil DNA glycosylase in complex with a protein inhibitor: Protein mimicry of DNA
    • Mol,C.D., Arvai,A.S., Sanderson,R.J., Slupphaug,G., Kavli,B., Krokan,H.E., Mosbaugh,D.W. and Tainer,J.A. (1995) Crystal structure of human uracil DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA. Cell, 82, 701-708.
    • (1995) Cell , vol.82 , pp. 701-708
    • Mol, C.D.1    Arvai, A.S.2    Sanderson, R.J.3    Slupphaug, G.4    Kavli, B.5    Krokan, H.E.6    Mosbaugh, D.W.7    Tainer, J.A.8
  • 26
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • Mol,C.D., Arvai,A.S., Slupphaug,G., Kavli,B., Alseth,I., Krokan,H.E. and Tainer,J.A. (1995) Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell, 80, 869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 27
    • 0345549815 scopus 로고
    • A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions
    • Cupples,C.G. and Miller,J.H. (1989) A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions. Proc. Natl Acad. Sci. USA, 86, 5345-5349.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5345-5349
    • Cupples, C.G.1    Miller, J.H.2
  • 28
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel,T.A., Bebenek,K. and McClary,J. (1991) Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol., 204, 125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 29
    • 0025240665 scopus 로고
    • Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites
    • Boiteux,S., O'Connor,T.R., Lederer,F., Gouyette,A. and Laval,J. (1990) Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites. J. Biol. Chem., 265, 3916-3922.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3916-3922
    • Boiteux, S.1    O'Connor, T.R.2    Lederer, F.3    Gouyette, A.4    Laval, J.5
  • 30
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • Nilsen,H., Otterlei,M., Haug,T., Solum,K., Nagelhus,T.A., Skorpen,F. and Krokan,H.E. (1997) Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. Nucleic Acids Res., 25, 750-755.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 31
    • 0027328401 scopus 로고
    • Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins
    • Castaing,B., Geiger,A., Seliger,H., Nehls,P., Laval,J., Zelwer,C. and Boiteux,S. (1993) Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins. Nucleic Acids Res., 21, 2899-2905.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2899-2905
    • Castaing, B.1    Geiger, A.2    Seliger, H.3    Nehls, P.4    Laval, J.5    Zelwer, C.6    Boiteux, S.7
  • 33
    • 0035071566 scopus 로고    scopus 로고
    • Bioterrorism: Implications for the clinical microbiologist
    • Klietmann,W.F. and Ruoff,K.L. (2001) Bioterrorism: implications for the clinical microbiologist. Clin. Microbiol. Rev., 14, 364-381.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 364-381
    • Klietmann, W.F.1    Ruoff, K.L.2
  • 34
    • 0034999808 scopus 로고    scopus 로고
    • The threat of smallpox and bioterrorism
    • Berche,P. (2001) The threat of smallpox and bioterrorism. Trends Microbiol., 9, 15-18.
    • (2001) Trends Microbiol. , vol.9 , pp. 15-18
    • Berche, P.1
  • 36
    • 0036677591 scopus 로고    scopus 로고
    • Emergency response to a smallpox attack: The case for mass vaccination
    • Kaplan,E.H., Craft,D.L. and Wein,L.M. (2002) Emergency response to a smallpox attack: the case for mass vaccination. Proc. Natl Acad. Sci. USA, 99, 10935-10940.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10935-10940
    • Kaplan, E.H.1    Craft, D.L.2    Wein, L.M.3
  • 38
    • 0022431831 scopus 로고
    • Excision of uracil residues in DNA: Mechanism of action of Escherichia coli and Micrococcus luteus uracil-DNA glycosylases
    • Delort,A.M., Duplaa,A.M., Molko,D., Teoule,R., Leblanc,J.P. and Laval,J. (1985) Excision of uracil residues in DNA: mechanism of action of Escherichia coli and Micrococcus luteus uracil-DNA glycosylases. Nucleic Acids Res., 13, 319-335.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 319-335
    • Delort, A.M.1    Duplaa, A.M.2    Molko, D.3    Teoule, R.4    Leblanc, J.P.5    Laval, J.6
  • 39
    • 0035421186 scopus 로고    scopus 로고
    • Excision of deaminated cytosine from the vertebrate genome: Role of the SMUG1 uracil-DNA glycosylase
    • Nilsen,H., Haushalter,K.A., Robins,P., Barnes,D.E., Verdine,G.L. and Lindahl,T. (2001) Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase. EMBO J., 20, 4278-4286.
    • (2001) EMBO J. , vol.20 , pp. 4278-4286
    • Nilsen, H.1    Haushalter, K.A.2    Robins, P.3    Barnes, D.E.4    Verdine, G.L.5    Lindahl, T.6
  • 40
    • 0035139061 scopus 로고    scopus 로고
    • Role of vaccinia virus A20R protein in DNA replication: Construction and characterization of temperature-sensitive mutants
    • Ishii,K. and Moss,B. (2001) Role of vaccinia virus A20R protein in DNA replication: construction and characterization of temperature-sensitive mutants. J. Virol., 75, 1656-1663.
    • (2001) J. Virol. , vol.75 , pp. 1656-1663
    • Ishii, K.1    Moss, B.2
  • 41
    • 0034712955 scopus 로고    scopus 로고
    • Genome-wide analysis of vaccinia virus protein-protein interactions
    • McCraith,S., Holtzman,T., Moss,B. and Fields,S. (2000) Genome-wide analysis of vaccinia virus protein-protein interactions. Proc. Natl Acad. Sci. USA, 97, 4879-4884.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4879-4884
    • McCraith, S.1    Holtzman, T.2    Moss, B.3    Fields, S.4
  • 42
    • 0035198155 scopus 로고    scopus 로고
    • The A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymerase
    • Klemperer,N., McDonald,W., Boyle,K., Unger,B. and Traktman,P. (2001) The A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymerase. J. Virol., 75, 12298-12307.
    • (2001) J. Virol. , vol.75 , pp. 12298-12307
    • Klemperer, N.1    McDonald, W.2    Boyle, K.3    Unger, B.4    Traktman, P.5
  • 43
    • 0035201672 scopus 로고    scopus 로고
    • Clustered charge-to-alanine mutagenesis of the vaccinia virus A20 gene: Temperature-sensitive mutants have a DNA-minus phenotype and are defective in the production of processive DNA polymerase activity
    • Punjabi,A., Boyle,K., DeMasi,J., Grubisha,O., Unger,B., Khanna,M. and Traktman,P. (2001) Clustered charge-to-alanine mutagenesis of the vaccinia virus A20 gene: temperature-sensitive mutants have a DNA-minus phenotype and are defective in the production of processive DNA polymerase activity. J. Virol., 75, 12308-12318.
    • (2001) J. Virol. , vol.75 , pp. 12308-12318
    • Punjabi, A.1    Boyle, K.2    DeMasi, J.3    Grubisha, O.4    Unger, B.5    Khanna, M.6    Traktman, P.7
  • 45
    • 0023014108 scopus 로고
    • Physical association of the human base-excision repair enzyme uracil DNA glycosylase with the 70,000-dalton catalytic subunit of DNA polymerase alpha
    • Seal,G. and Sirover,M.A. (1986) Physical association of the human base-excision repair enzyme uracil DNA glycosylase with the 70,000-dalton catalytic subunit of DNA polymerase alpha. Proc. Natl Acad. Sci. USA, 83, 7608-7612.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7608-7612
    • Seal, G.1    Sirover, M.A.2


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