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Volumn 383, Issue 3, 1997, Pages 189-196

DNA glycosylases

Author keywords

AP endonuclease; AP lyase; Base excision repair; DNA glycosylase; DNA repair

Indexed keywords

DNA GLYCOSYLTRANSFERASE;

EID: 0030979263     PISSN: 09218777     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0921-8777(97)00008-6     Document Type: Review
Times cited : (96)

References (45)
  • 1
    • 0028675314 scopus 로고
    • Reconstitution of the DNA base excision-repair pathway
    • Dianov, G. and T. Lindahl (1994) Reconstitution of the DNA base excision-repair pathway, Curr. Biol., 4, 1069-1076.
    • (1994) Curr. Biol. , vol.4 , pp. 1069-1076
    • Dianov, G.1    Lindahl, T.2
  • 3
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • Doetsch, P.W. and R.P. Cunningham (1990) The enzymology of apurinic/apyrimidinic endonucleases, Mutation Res. DNA Repair, 236, 173-201.
    • (1990) Mutation Res. DNA Repair , vol.236 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 4
    • 0023127167 scopus 로고
    • Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst
    • Bailly, V. and W.G. Verly (1987) Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst, Biochem. J., 242, 565-572.
    • (1987) Biochem. J. , vol.242 , pp. 565-572
    • Bailly, V.1    Verly, W.G.2
  • 6
    • 0026101901 scopus 로고
    • Stereochemical studies of the β-elimination reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys
    • Mazumder, A., J.A. Gerlt, M.J. Absalon, J. Stubbe, R.P. Cunningham, J. Withka and P.H. Bolton (1991) Stereochemical studies of the β-elimination reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys, Biochemistry, 30, 1116-1126.
    • (1991) Biochemistry , vol.30 , pp. 1116-1126
    • Mazumder, A.1    Gerlt, J.A.2    Absalon, M.J.3    Stubbe, J.4    Cunningham, R.P.5    Withka, J.6    Bolton, P.H.7
  • 7
    • 0030053998 scopus 로고    scopus 로고
    • 3′ and 5′-strand cleavage reactions catalyzed by the Fpg protein from Escherichia coli occur via successive β- And δ-elimination mechanisms respectively
    • Bhagwat, M. and J.A. Gerlt (1996) 3′ and 5′-strand cleavage reactions catalyzed by the Fpg protein from Escherichia coli occur via successive β- and δ-elimination mechanisms respectively, Biochemistry, 35, 659-665.
    • (1996) Biochemistry , vol.35 , pp. 659-665
    • Bhagwat, M.1    Gerlt, J.A.2
  • 8
    • 0028982164 scopus 로고
    • δ-Elimination by T4 endonuclease V at a thymine dimer site requires a secondary binding event and amino acid Glu-23
    • Latham, K.A. and R.S. Lloyd (1995) δ-Elimination by T4 endonuclease V at a thymine dimer site requires a secondary binding event and amino acid Glu-23, Biochemistry, 34, 8796-8803.
    • (1995) Biochemistry , vol.34 , pp. 8796-8803
    • Latham, K.A.1    Lloyd, R.S.2
  • 9
    • 0029132769 scopus 로고
    • Studies on the catalytic mechanism of five DNA glycosylases. Probing for enzyme-DNA imino intermediates
    • Sun, B., K.A. Latham, M.L. Dodson and R.S. Lloyd (1995) Studies on the catalytic mechanism of five DNA glycosylases. Probing for enzyme-DNA imino intermediates, J. Biol. Chem., 270, 19501-19508.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19501-19508
    • Sun, B.1    Latham, K.A.2    Dodson, M.L.3    Lloyd, R.S.4
  • 10
    • 0029013243 scopus 로고
    • The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site
    • Tchou, J. and A.P. Grollman (1995) The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site, J. Biol. Chem., 270, 11671-11677.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11671-11677
    • Tchou, J.1    Grollman, A.P.2
  • 11
    • 0030890419 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III
    • in press
    • Hilbert, T.P., W. Chaung, R.J. Boorstein, R.P. Cunningham and G.W. Teebor (1997) Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III, J. Biol. Chem., in press.
    • (1997) J. Biol. Chem.
    • Hilbert, T.P.1    Chaung, W.2    Boorstein, R.J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 12
    • 0027301692 scopus 로고
    • Evidence for an imino intermediate in the T4 endonuclease V reaction
    • Dodson, M.L., R.D. Schrock and R.S. Lloyd (1993) Evidence for an imino intermediate in the T4 endonuclease V reaction, Biochemistry, 32, 8284-8290.
    • (1993) Biochemistry , vol.32 , pp. 8284-8290
    • Dodson, M.L.1    Schrock, R.D.2    Lloyd, R.S.3
  • 13
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer, M.M., H. Ahern, D. Xing, R.P. Cunningham and J.A. Tainer (1995) Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure, EMBO J., 14, 4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 14
    • 0029743301 scopus 로고    scopus 로고
    • Base excision of oxidative purine and pyrimidine DNa damage in Saccharomyces cerevisiae by a DNa glycosylase with sequence similarity to endonuclease III from Escherichia coli
    • Eide, L., M. Bjørås, M. Pirovano, I. Alseth, K.G. Berdal and E. Seeberg (1996) Base excision of oxidative purine and pyrimidine DNA damage in Saccharomyces cerevisiae by a DNA glycosylase with sequence similarity to endonuclease III from Escherichia coli, Proc. Natl. Acad. Sci. USA, 93, 10735-10740.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10735-10740
    • Eide, L.1    Bjørås, M.2    Pirovano, M.3    Alseth, I.4    Berdal, K.G.5    Seeberg, E.6
  • 15
    • 0029814011 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a Schizosaccacaromyces pombe homologue of Escherichia coli endonuclease III
    • Roldán-Arjona T., A.C. Anselmino and T. Lindahl (1996) Molecular cloning and functional analysis of a Schizosaccacaromyces pombe homologue of Escherichia coli endonuclease III, Nucleic Acids Res., 24, 3307-3312.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3307-3312
    • Roldán-Arjona, T.1    Anselmino, A.C.2    Lindahl, T.3
  • 16
    • 5544239019 scopus 로고    scopus 로고
    • Purification of a mammalian homologue of Escherichia coli endonuclease III: Identification of a bovine pyrimidine hydrate thymine glycol DNA-glycosylase AP lyase by irreversible cross linking to a thymine glycol-containing oligodeoxynucleotide
    • Hilbert, T.P., R.J. Boorstein, H.C. Kung, P.H. Bolton, D. Xing, R.P. Cunningham and G.W. Teebor (1996) Purification of a mammalian homologue of Escherichia coli endonuclease III: identification of a bovine pyrimidine hydrate thymine glycol DNA-glycosylase AP lyase by irreversible cross linking to a thymine glycol-containing oligodeoxynucleotide, Biochemistry, 35, 2505-2511.
    • (1996) Biochemistry , vol.35 , pp. 2505-2511
    • Hilbert, T.P.1    Boorstein, R.J.2    Kung, H.C.3    Bolton, P.H.4    Xing, D.5    Cunningham, R.P.6    Teebor, G.W.7
  • 17
    • 0016692306 scopus 로고
    • Endonucleolytic incision of X-irradiated deoxyribonucleic acid by extracts of Escherichia coli
    • Strniste, G.F. and S.S. Wallace (1975) Endonucleolytic incision of X-irradiated deoxyribonucleic acid by extracts of Escherichia coli, Proc. Natl. Acad. Sci. USA, 72, 1997-2001.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1997-2001
    • Strniste, G.F.1    Wallace, S.S.2
  • 18
    • 0018926091 scopus 로고
    • DNA N-glycosylases and UV repair
    • Demple, B. and S. Linn (1980) DNA N-glycosylases and UV repair, Nature, 287, 203-208.
    • (1980) Nature , vol.287 , pp. 203-208
    • Demple, B.1    Linn, S.2
  • 19
    • 0021331957 scopus 로고
    • DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli
    • Breimer, L.H. and T. Lindahl (1984) DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli, J. Biol. Chem., 259, 5543-5548.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5543-5548
    • Breimer, L.H.1    Lindahl, T.2
  • 20
    • 0028305721 scopus 로고
    • New substrates for old enzymes. 5-hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNa N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNa N-glycosylase
    • Hatahet, Z., Y.W. Kow, A.A. Purmal, R.P. Cunningham and S.S. Wallace (1994) New substrates for old enzymes. 5-hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase, J. Biol. Chem., 269, 18814-18820.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18814-18820
    • Hatahet, Z.1    Kow, Y.W.2    Purmal, A.A.3    Cunningham, R.P.4    Wallace, S.S.5
  • 21
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • Doherty, A.J., L.C. Serpell and C.P. Ponting (1996) The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA, Nucleic Acids Res., 24, 2488-2498.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2488-2498
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 22
    • 0028800939 scopus 로고
    • Purification and cloning of Micrococcus luteus ultraviolet endonuclease, an N-glycosylase abasic lyase that proceeds via an imino enzyme-DNA intermediate
    • Piersen, C.E., M.A. Prince, M.L. Augustine, M.L. Dodson and R.S. Lloyd (1995) Purification and cloning of Micrococcus luteus ultraviolet endonuclease, an N-glycosylase abasic lyase that proceeds via an imino enzyme-DNA intermediate, J. Biol. Chem., 270, 23475-23484.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23475-23484
    • Piersen, C.E.1    Prince, M.A.2    Augustine, M.L.3    Dodson, M.L.4    Lloyd, R.S.5
  • 23
    • 0029834498 scopus 로고    scopus 로고
    • Counteracting the mutagenic effect of hydrolytic deamination of DNA 5-methylcytosine residues at high temperature: DNA mismatch N-glycosylase Mig. Mth of the thermophilic archaeon Methanobacterium thermoautotrophicum THF
    • Horst, J.-P. and H.-J. Fritz (1996) Counteracting the mutagenic effect of hydrolytic deamination of DNA 5-methylcytosine residues at high temperature: DNA mismatch N-glycosylase Mig. Mth of the thermophilic archaeon Methanobacterium thermoautotrophicum THF, EMBO J., 15, 5459-5469.
    • (1996) EMBO J. , vol.15 , pp. 5459-5469
    • Horst, J.-P.1    Fritz, H.-J.2
  • 24
    • 0024332124 scopus 로고
    • Escherichia coli mutY gene encodes an adenine glycosylase active on GA mispairs
    • Au, K.G., S. Clark, J.H. Miller and P. Modrich (1989) Escherichia coli mutY gene encodes an adenine glycosylase active on GA mispairs, Proc. Natl. Acad. Sci. USA, 86, 8877-8881.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8877-8881
    • Au, K.G.1    Clark, S.2    Miller, J.H.3    Modrich, P.4
  • 25
    • 0025301064 scopus 로고
    • MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III
    • Michaels, M.L., L. Pham, Y. Nghiem, C. Cruz and J.H. Miller (1990) MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III, Nucleic Acids Res., 18, 3841-3845.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Nghiem, Y.3    Cruz, C.4    Miller, J.H.5
  • 26
    • 0026703168 scopus 로고
    • Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A·C and A·G mispairs
    • Tsai-Wu, J., H. Liu and A. Lu (1992) Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A·C and A·G mispairs, Proc. Natl. Acad. Sci. USA, 89, 8779-8783.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8779-8783
    • Tsai-Wu, J.1    Liu, H.2    Lu, A.3
  • 27
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNa damage
    • Slupska, M.M., C. Baikalov, W.M. Luther, J.H. Chiang, Y.F. Wei and J.H. Miller (1996) Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage, J. Bacteriol., 178, 3885-3892.
    • (1996) J. Bacteriol. , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.H.4    Wei, Y.F.5    Miller, J.H.6
  • 30
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNa glycosylase reveals the existence of a base-excision DNA-repair protein super-family
    • Nash, H.W., S.D. Bruner, O.D. Schärer, T. Kawate, T.A. Addona, E. Spooner, W.S. Lane and G.L. Verdine (1996) Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein super-family, Curr. Biol., 6, 968-980.
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.W.1    Bruner, S.D.2    Schärer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 31
    • 0029896229 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNa glycosylase that excises 7,8 dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine
    • Aufret van der Kamp, P., D. Thomas, R. Barbey, R. de Oliveira and S. Boiteux (1996) Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8 dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine, Proc. Natl. Acad. Sci. USA, 93, 5197-5202.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5197-5202
    • Aufret Van Der Kamp, P.1    Thomas, D.2    Barbey, R.3    De Oliveira, R.4    Boiteux, S.5
  • 33
    • 0029805081 scopus 로고    scopus 로고
    • A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase
    • Gallinari, P. and J. Jiricny (1996) A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase, Nature, 383, 735738.
    • (1996) Nature , vol.383 , pp. 735738
    • Gallinari, P.1    Jiricny, J.2
  • 34
    • 0028295382 scopus 로고
    • Isolation and characterization of endonuclease VIII from Escherichia coli
    • Melamede, R.J., Z. Hatahet, Y.W. Kow, H. Ide and, S.S. Wallace (1994) Isolation and characterization of endonuclease VIII from Escherichia coli, Biochemistry, 33, 1255-1264.
    • (1994) Biochemistry , vol.33 , pp. 1255-1264
    • Melamede, R.J.1    Hatahet, Z.2    Kow, Y.W.3    Ide, H.4    Wallace, S.S.5
  • 35
    • 0027462131 scopus 로고
    • Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role
    • O'Connor, T.R., R.J. Graves, G. de Murcia, B. Castaing and J. Laval (1993) Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role, J. Biol. Chem., 268, 9063-9070.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9063-9070
    • O'Connor, T.R.1    Graves, R.J.2    De Murcia, G.3    Castaing, B.4    Laval, J.5
  • 36
    • 0027370887 scopus 로고
    • Function of the zinc finger in Escherichia coli Fpg protein
    • Tchou, J., M.L. Michaels, J.H. Miller and A.P. Grollman (1993) Function of the zinc finger in Escherichia coli Fpg protein, J. Biol. Chem., 268, 26738-26744.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26738-26744
    • Tchou, J.1    Michaels, M.L.2    Miller, J.H.3    Grollman, A.P.4
  • 37
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • Mol, C.D., A.S. Arvai, G. Slupphaug, B. Kavli, I. Alseth, H.E. Krokan and J.A. Tainer (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
  • 38
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracilDNA glycosylase
    • Saava, R., K. McAuley-Hecht, T. Brown and L. Pearl (1995) The structural basis of specific base-excision repair by uracilDNA glycosylase, Nature, 373, 487-493.
    • (1995) Nature , vol.373 , pp. 487-493
    • Saava, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 39
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimasauskas, S., S. Kumar, R.J. Roberts and X. Cheng (1994) HhaI methyltransferase flips its target base out of the DNA helix, Cell, 76, 357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 40
    • 0029068629 scopus 로고
    • The crystal structure of HaeIII methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing
    • Reinish, K.M., L. Chen, G.L. Verdine and W.N. Lipscomb (1995) The crystal structure of HaeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing, Cell, 82, 143-153.
    • (1995) Cell , vol.82 , pp. 143-153
    • Reinish, K.M.1    Chen, L.2    Verdine, G.L.3    Lipscomb, W.N.4
  • 42
    • 0028863468 scopus 로고
    • Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNa substrate: Structural basis for damaged DNa recognition
    • Vassylvev, D.G., T. Kashiwagi, Y. Mikami, M. Ariyoshi, S. Iwai, E. Ohtsuka and K. Morikawa (1995) Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition, Cell, 83, 773-782.
    • (1995) Cell , vol.83 , pp. 773-782
    • Vassylvev, D.G.1    Kashiwagi, T.2    Mikami, Y.3    Ariyoshi, M.4    Iwai, S.5    Ohtsuka, E.6    Morikawa, K.7
  • 43
    • 0029068245 scopus 로고
    • On base flipping
    • Roberts, R.J. (1995) On base flipping, Cell, 82, 9-12.
    • (1995) Cell , vol.82 , pp. 9-12
    • Roberts, R.J.1
  • 44
    • 0030585418 scopus 로고    scopus 로고
    • Finding a basis for flipping bases
    • Cheng, X. and R.M. Blumehthal (1996) Finding a basis for flipping bases, Structure, 4, 639-645.
    • (1996) Structure , vol.4 , pp. 639-645
    • And, C.X.1    Blumehthal, R.M.2
  • 45
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • Slupphaug, G., C.D. Mol, B. Kavli, A.S. Arvai, H.E. Krokan and J.A. Tainer (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.