메뉴 건너뛰기




Volumn 3, Issue 1, 2004, Pages 1-12

Abasic sites in DNA: Repair and biological consequences in Saccharomyces cerevisiae

Author keywords

Apurinic apyrimidinic sites; DNA repair; DNA single strand breaks; Saccharomyces cerevisiae

Indexed keywords

DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA DIRECTED DNA POLYMERASE DELTA; LYASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 0348140585     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2003.10.002     Document Type: Short Survey
Times cited : (412)

References (87)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature. 362:1993;709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers J.H. Genome maintenance mechanisms for preventing cancer. Nature. 411:2001;366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 3
    • 85015066476 scopus 로고    scopus 로고
    • DNA damage and repair
    • Friedberg E.C. DNA damage and repair. Nature. 421:2003;436-440.
    • (2003) Nature , vol.421 , pp. 436-440
    • Friedberg, E.C.1
  • 4
    • 0015504248 scopus 로고
    • Rate of depurination of native deoxyribonucleic acid
    • Lindahl T., Nyberg B. Rate of depurination of native deoxyribonucleic acid. Biochemistry. 11:1972;3610-3618.
    • (1972) Biochemistry , vol.11 , pp. 3610-3618
    • Lindahl, T.1    Nyberg, B.2
  • 5
    • 0015504253 scopus 로고
    • Rate of chain breakage at apurinic sites in double-stranded deoxyribonucleic acid
    • Lindahl T., Andersson A. Rate of chain breakage at apurinic sites in double-stranded deoxyribonucleic acid. Biochemistry. 11:1972;3618-3623.
    • (1972) Biochemistry , vol.11 , pp. 3618-3623
    • Lindahl, T.1    Andersson, A.2
  • 6
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan H.E., Standal R., Slupphaug G. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325:1997;1-16.
    • (1997) Biochem. J. , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 7
    • 0035111895 scopus 로고    scopus 로고
    • Recent progress in the biology, chemistry and structural biology of DNA glycosylases
    • Scharer O.D., Jiricny J. Recent progress in the biology, chemistry and structural biology of DNA glycosylases. Bioessays. 23:2001;270-281.
    • (2001) Bioessays , vol.23 , pp. 270-281
    • Scharer, O.D.1    Jiricny, J.2
  • 9
    • 0020341190 scopus 로고
    • Nonenzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-L-methionine is a potentially mutagenic reaction
    • Rydberg B., Lindahl T. Nonenzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-L-methionine is a potentially mutagenic reaction. EMBO J. 1:1982;211-216.
    • (1982) EMBO J. , vol.1 , pp. 211-216
    • Rydberg, B.1    Lindahl, T.2
  • 10
    • 0016257644 scopus 로고
    • Heat-induced deamination of cytosine residues in deoxyribonucleic acid
    • Lindahl T., Nyberg B. Heat-induced deamination of cytosine residues in deoxyribonucleic acid. Biochemistry. 13:1974;3405-3410.
    • (1974) Biochemistry , vol.13 , pp. 3405-3410
    • Lindahl, T.1    Nyberg, B.2
  • 11
    • 0024508509 scopus 로고
    • Uracil DNA glycosylases and DNA uracil repair
    • Tomilin N.V., Aprelikova O.N. Uracil DNA glycosylases and DNA uracil repair. Int. Rev. Cytol. 114:1989;125-179.
    • (1989) Int. Rev. Cytol. , vol.114 , pp. 125-179
    • Tomilin, N.V.1    Aprelikova, O.N.2
  • 12
    • 0033152195 scopus 로고    scopus 로고
    • Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues
    • Nakamura J., Swenberg J.A. Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues. Cancer Res. 59:1999;2522-2526.
    • (1999) Cancer Res. , vol.59 , pp. 2522-2526
    • Nakamura, J.1    Swenberg, J.A.2
  • 13
    • 0022037404 scopus 로고
    • Apurinic sites as mutagenic intermediates
    • Loeb L.A. Apurinic sites as mutagenic intermediates. Cell. 40:1985;483-484.
    • (1985) Cell , vol.40 , pp. 483-484
    • Loeb, L.A.1
  • 14
    • 0034675927 scopus 로고    scopus 로고
    • Repair of chromosomal abasic sites in vivo involves at least three different repair pathways
    • Otterlei M., Kavli B., Standal R., Skjelbred C., Bharati S., Krokan H.E. Repair of chromosomal abasic sites in vivo involves at least three different repair pathways. EMBO J. 19:2000;5542-5551.
    • (2000) EMBO J. , vol.19 , pp. 5542-5551
    • Otterlei, M.1    Kavli, B.2    Standal, R.3    Skjelbred, C.4    Bharati, S.5    Krokan, H.E.6
  • 15
    • 0036682979 scopus 로고    scopus 로고
    • Translesion DNA synthesis in eukaryotes: A one- or twopolymerase affair
    • Prakash S., Prakash L. Translesion DNA synthesis in eukaryotes: a one- or twopolymerase affair. Genes Dev. 16:2002;1872-1883.
    • (2002) Genes Dev. , vol.16 , pp. 1872-1883
    • Prakash, S.1    Prakash, L.2
  • 16
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple B., Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63:1994;915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 17
    • 0035009313 scopus 로고    scopus 로고
    • Mammalian DNA single-strand break repair: An X-ra(y)ted affair
    • Caldecott K.W. Mammalian DNA single-strand break repair: an X-ra(y)ted affair. Bioessays. 23:2001;447-455.
    • (2001) Bioessays , vol.23 , pp. 447-455
    • Caldecott, K.W.1
  • 19
    • 0037310197 scopus 로고    scopus 로고
    • Disparity between DNA base excision repair in yeast and mammals: Translational implications
    • Kelley M.R., Kow Y.W., Wilson D.M. 3rd Disparity between DNA base excision repair in yeast and mammals: translational implications. Cancer Res. 63:2003;549-554.
    • (2003) Cancer Res. , vol.63 , pp. 549-554
    • Kelley, M.R.1    Kow, Y.W.2    Wilson III, D.M.3
  • 20
    • 0034733692 scopus 로고    scopus 로고
    • Yeast DNA repair and human implications: Past, present and future perspectives on DNA repair in yeast
    • (special issue)
    • Resnick M.A., Cox B.S. Yeast DNA repair and human implications: past, present and future perspectives on DNA repair in yeast. Mutat. Res. 451:2000;1-295. (special issue).
    • (2000) Mutat. Res. , vol.451 , pp. 1-295
    • Resnick, M.A.1    Cox, B.S.2
  • 21
    • 0033557310 scopus 로고    scopus 로고
    • Relationships between yeast Rad27 and Apn1 in response to apurinic/apyrimidinic (AP) sites in DNA
    • Wu X., Wang Z. Relationships between yeast Rad27 and Apn1 in response to apurinic/apyrimidinic (AP) sites in DNA. Nucleic Acids Res. 27:1999;956-962.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 956-962
    • Wu, X.1    Wang, Z.2
  • 22
    • 0027475974 scopus 로고
    • DNA repair synthesis during base excision repair in vitro is catalyzed by DNA polymerase epsilon and is influenced by DNA polymerases alpha and delta in Saccharomyces cerevisiae
    • Wang Z., Wu X., Friedberg E.C. DNA repair synthesis during base excision repair in vitro is catalyzed by DNA polymerase epsilon and is influenced by DNA polymerases alpha and delta in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1993;1051-1058.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1051-1058
    • Wang, Z.1    Wu, X.2    Friedberg, E.C.3
  • 23
    • 0025324303 scopus 로고
    • Yeast structural gene (APN1) for the major apurinic endonuclease: Homology to Escherichia coli endonuclease IV
    • Popoff S.C., Spira A.I., Johnson A.W., Demple B. Yeast structural gene (APN1) for the major apurinic endonuclease: homology to Escherichia coli endonuclease IV. Proc. Natl. Acad. Sci. U.S.A. 87:1990;4193-4197.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4193-4197
    • Popoff, S.C.1    Spira, A.I.2    Johnson, A.W.3    Demple, B.4
  • 24
    • 0025864553 scopus 로고
    • Cellular role of yeast Apn1 apurinic endonuclease/3′-diesterase: Repair of oxidative and alkylation DNA damage and control of spontaneous mutation
    • Ramotar D., Popoff S.C., Gralla E.B., Demple B. Cellular role of yeast Apn1 apurinic endonuclease/3′-diesterase: repair of oxidative and alkylation DNA damage and control of spontaneous mutation. Mol. Cell. Biol. 11:1991;4537-4544.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4537-4544
    • Ramotar, D.1    Popoff, S.C.2    Gralla, E.B.3    Demple, B.4
  • 25
    • 0026335385 scopus 로고
    • Metalloenzymes in DNA repair: Escherichia coli endonuclease IV and Saccharomyces cerevisiae Apn1
    • Levin J., Shapiro R., Demple B. Metalloenzymes in DNA repair: Escherichia coli endonuclease IV and Saccharomyces cerevisiae Apn1. J. Biol. Chem. 266:1991;22893-22898.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22893-22898
    • Levin, J.1    Shapiro, R.2    Demple, B.3
  • 26
    • 0027218970 scopus 로고
    • Intracellular localization of the Apn1 DNA repair enzyme of Saccharomyces cerevisiae: Nuclear transport signals and biological role
    • Ramotar D., Kim C., Lillis R., Demple B. Intracellular localization of the Apn1 DNA repair enzyme of Saccharomyces cerevisiae: nuclear transport signals and biological role. J. Biol. Chem. 268:1993;20533-20539.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20533-20539
    • Ramotar, D.1    Kim, C.2    Lillis, R.3    Demple, B.4
  • 27
    • 0035137178 scopus 로고    scopus 로고
    • Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability
    • Vongsamphanh R., Fortier P.K., Ramotar D. Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability. Mol. Cell. Biol. 21:2001;1647-1655.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1647-1655
    • Vongsamphanh, R.1    Fortier, P.K.2    Ramotar, D.3
  • 28
    • 0024279593 scopus 로고
    • Yeast DNA diesterase for 3′-fragments of deoxyribose: Purification and physical properties of a repair enzyme for oxidative DNA damage
    • Johnson A.W., Demple B. Yeast DNA diesterase for 3′-fragments of deoxyribose: purification and physical properties of a repair enzyme for oxidative DNA damage. J. Biol. Chem. 263:1988;18009-18016.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18009-18016
    • Johnson, A.W.1    Demple, B.2
  • 29
    • 0024279616 scopus 로고
    • Yeast DNA 3′-repair diesterase is the major cellular apurinic/apyrimidinic endonuclease: Substrate specificity and kinetics
    • Johnson A.W., Demple B. Yeast DNA 3′-repair diesterase is the major cellular apurinic/apyrimidinic endonuclease: substrate specificity and kinetics. J. Biol. Chem. 263:1988;18017-18022.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18017-18022
    • Johnson, A.W.1    Demple, B.2
  • 30
    • 0037069381 scopus 로고    scopus 로고
    • Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1
    • Liu C., Pouliot J.J., Nash H.A. Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1. Proc. Natl. Acad. Sci. U.S.A. 99:2002;14970-14975.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14970-14975
    • Liu, C.1    Pouliot, J.J.2    Nash, H.A.3
  • 31
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko A.A., Saparbaev M.K. Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature. 415:2002;183-187.
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 32
    • 0034785884 scopus 로고    scopus 로고
    • Repair of DNA strand breaks by the overlapping functions of lesion-specific and non-lesion-specific DNA 3′ phosphatases
    • Vance J.R., Wilson T.E. Repair of DNA strand breaks by the overlapping functions of lesion-specific and non-lesion-specific DNA 3′ phosphatases. Mol. Cell. Biol. 21:2001;7191-7198.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7191-7198
    • Vance, J.R.1    Wilson, T.E.2
  • 33
    • 0032913570 scopus 로고    scopus 로고
    • Overlapping specificities of base excision repair, nucleotide excision repair, recombination, and translesion synthesis pathways for DNA base damage in Saccharomyces cerevisiae
    • Swanson R.L., Morey N.J., Doetsch P.W., Jinks-Robertson S. Overlapping specificities of base excision repair, nucleotide excision repair, recombination, and translesion synthesis pathways for DNA base damage in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:1999;2929-2935.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2929-2935
    • Swanson, R.L.1    Morey, N.J.2    Doetsch, P.W.3    Jinks-Robertson, S.4
  • 34
    • 0027477075 scopus 로고
    • In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells
    • Xiao W., Samson L. In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells. Proc. Natl. Acad. Sci. U.S.A. 90:1993;2117-2121.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2117-2121
    • Xiao, W.1    Samson, L.2
  • 35
    • 0032190633 scopus 로고    scopus 로고
    • Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites
    • Johnson R.E., Torres-Ramos C.A., Izumi T., Mitra S., Prakash S., Prakash L. Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites. Genes Dev. 12:1998;3137-3143.
    • (1998) Genes Dev. , vol.12 , pp. 3137-3143
    • Johnson, R.E.1    Torres-Ramos, C.A.2    Izumi, T.3    Mitra, S.4    Prakash, S.5    Prakash, L.6
  • 36
    • 0030611925 scopus 로고    scopus 로고
    • Partial purification of Pde1 from Saccharomyces cerevisiae: Enzymatic redundancy for the repair of 3′-terminal DNA lesions and abasic sites in yeast
    • Sander M., Ramotar D. Partial purification of Pde1 from Saccharomyces cerevisiae: enzymatic redundancy for the repair of 3′-terminal DNA lesions and abasic sites in yeast. Biochemistry. 36:1997;6100-6106.
    • (1997) Biochemistry , vol.36 , pp. 6100-6106
    • Sander, M.1    Ramotar, D.2
  • 37
    • 0032980426 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis
    • Bennett R.A. The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis. Mol. Cell. Biol. 19:1999;1800-1809.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1800-1809
    • Bennett, R.A.1
  • 38
    • 0036303482 scopus 로고    scopus 로고
    • Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III
    • Hadi M.Z., Ginalski K., Nguyen L.H., Wilson D.M. 3rd Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III. J. Mol. Biol. 316:2002;853-866.
    • (2002) J. Mol. Biol. , vol.316 , pp. 853-866
    • Hadi, M.Z.1    Ginalski, K.2    Nguyen, L.H.3    Wilson III, D.M.4
  • 40
    • 0036707526 scopus 로고    scopus 로고
    • Stimulation of 3′ → 5′ exonuclease and 3′-phosphodiesterase activities of yeast Apn2 by proliferating cell nuclear antigen
    • Unk I., Haracska L., Gomes X.V., Burgers P.M., Prakash L., Prakash S. Stimulation of 3′ → 5′ exonuclease and 3′- phosphodiesterase activities of yeast Apn2 by proliferating cell nuclear antigen. Mol. Cell. Biol. 22:2002;6480-6486.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6480-6486
    • Unk, I.1    Haracska, L.2    Gomes, X.V.3    Burgers, P.M.4    Prakash, L.5    Prakash, S.6
  • 41
    • 0034746231 scopus 로고    scopus 로고
    • 3′-Phosphodiesterase and 3′ → 5′ exonuclease activities of yeast Apn2 protein and requirement of these activities for repair of oxidative DNA damage
    • Unk I., Haracska L., Prakash S., Prakash L. 3′-Phosphodiesterase and 3′ → 5′ exonuclease activities of yeast Apn2 protein and requirement of these activities for repair of oxidative DNA damage. Mol. Cell. Biol. 21:2001;1656-1661.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1656-1661
    • Unk, I.1    Haracska, L.2    Prakash, S.3    Prakash, L.4
  • 42
    • 0035915411 scopus 로고    scopus 로고
    • Deletion of the MAG1 DNA glycosylase gene suppresses alkylation-induced killing and mutagenesis in yeast cells lacking AP endonucleases
    • Xiao W., Chow B.L., Hanna M., Doetsch P.W. Deletion of the MAG1 DNA glycosylase gene suppresses alkylation-induced killing and mutagenesis in yeast cells lacking AP endonucleases. Mutat. Res. 487:2001;137-147.
    • (2001) Mutat. Res. , vol.487 , pp. 137-147
    • Xiao, W.1    Chow, B.L.2    Hanna, M.3    Doetsch, P.W.4
  • 43
    • 0035805515 scopus 로고    scopus 로고
    • Uncoupling of 3′-phosphatase and 5′-kinase functions in budding yeast. Characterization of Saccharomyces cerevisiae DNA 3′-phosphatase (TPP1)
    • Vance J.R., Wilson T.E. Uncoupling of 3′-phosphatase and 5′-kinase functions in budding yeast. Characterization of Saccharomyces cerevisiae DNA 3′-phosphatase (TPP1). J. Biol. Chem. 276:2001;15073-15081.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15073-15081
    • Vance, J.R.1    Wilson, T.E.2
  • 44
    • 0031463790 scopus 로고    scopus 로고
    • Repair of oxidized DNA bases in the yeast Saccharomyces cerevisiae
    • Girard P.M., Boiteux S. Repair of oxidized DNA bases in the yeast Saccharomyces cerevisiae. Biochimie. 79:1997;559-566.
    • (1997) Biochimie , vol.79 , pp. 559-566
    • Girard, P.M.1    Boiteux, S.2
  • 46
    • 0032960862 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast
    • Alseth I., Eide L., Pirovano M., Rognes T., Seeberg E., Bjoras M. The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast. Mol. Cell. Biol. 19:1999;3779-3787.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3779-3787
    • Alseth, I.1    Eide, L.2    Pirovano, M.3    Rognes, T.4    Seeberg, E.5    Bjoras, M.6
  • 47
    • 0032401931 scopus 로고    scopus 로고
    • Substrate specificities of the Ntg1 and Ntg2 proteins of Saccharomyces cerevisiae for oxidized DNA bases are not identical
    • Senturker S., Auffret van der Kemp P., You H.J., Doetsch P.W., Dizdaroglu M., Boiteux S. Substrate specificities of the Ntg1 and Ntg2 proteins of Saccharomyces cerevisiae for oxidized DNA bases are not identical. Nucleic Acids Res. 26:1998;5270-5276.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5270-5276
    • Senturker, S.1    Auffret Van Der Kemp, P.2    You, H.J.3    Doetsch, P.W.4    Dizdaroglu, M.5    Boiteux, S.6
  • 48
    • 0030750215 scopus 로고    scopus 로고
    • The Ogg1 protein of Saccharomyces cerevisiae: A 7,8-dihydro-8-oxoguanine DNA N-glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activity
    • Girard P.M., Guibourt N., Boiteux S. The Ogg1 protein of Saccharomyces cerevisiae: a 7,8-dihydro-8-oxoguanine DNA N-glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activity. Nucleic Acids Res. 25:1997;3404-3411.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3404-3411
    • Girard, P.M.1    Guibourt, N.2    Boiteux, S.3
  • 49
    • 0037013854 scopus 로고    scopus 로고
    • Endogenous DNA abasic sites cause cell death in the absence of Apn1, Apn2 and Rad1/Rad10 in Saccharomyces cerevisiae
    • Guillet M., Boiteux S. Endogenous DNA abasic sites cause cell death in the absence of Apn1, Apn2 and Rad1/Rad10 in Saccharomyces cerevisiae. EMBO J. 21:2002;2833-2841.
    • (2002) EMBO J. , vol.21 , pp. 2833-2841
    • Guillet, M.1    Boiteux, S.2
  • 50
    • 0037177823 scopus 로고    scopus 로고
    • Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double flap structure as the cellular substrate
    • Kao H.-I., Henricksen L.A., Liu Y., Bambara R.A. Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double flap structure as the cellular substrate. J. Biol. Chem. 277:2002;14379-14389.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14379-14389
    • Kao, H.-I.1    Henricksen, L.A.2    Liu, Y.3    Bambara, R.A.4
  • 51
    • 0035692142 scopus 로고    scopus 로고
    • Overlapping functions of the Saccharomyces cerevisiae Mre11, Exo1 and Rad27 nucleases in DNA metabolism
    • Moreau S., Morgan E.A., Symington L.S. Overlapping functions of the Saccharomyces cerevisiae Mre11, Exo1 and Rad27 nucleases in DNA metabolism. Genetics. 159:2001;1423-1433.
    • (2001) Genetics , vol.159 , pp. 1423-1433
    • Moreau, S.1    Morgan, E.A.2    Symington, L.S.3
  • 52
    • 0027943565 scopus 로고
    • Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease
    • Bardwell A.J., Bardwell L., Tomkinson A.E., Friedberg E.C. Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease. Science. 265:1994;2082-2085.
    • (1994) Science , vol.265 , pp. 2082-2085
    • Bardwell, A.J.1    Bardwell, L.2    Tomkinson, A.E.3    Friedberg, E.C.4
  • 53
    • 0027225340 scopus 로고
    • Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease
    • Tomkinson A.E., Bardwell A.J., Bardwell L., Tappe N.J., Friedberg E.C. Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease. Nature. 362:1993;860-862.
    • (1993) Nature , vol.362 , pp. 860-862
    • Tomkinson, A.E.1    Bardwell, A.J.2    Bardwell, L.3    Tappe, N.J.4    Friedberg, E.C.5
  • 54
    • 0037965787 scopus 로고    scopus 로고
    • The mechanism of Mus81-Mms4 cleavage site selection distinguishes it from the homologous endonuclease Rad1-Rad10
    • Bastin-Shanower S.A., Fricke W.M., Mullen J.R., Brill S.J. The mechanism of Mus81-Mms4 cleavage site selection distinguishes it from the homologous endonuclease Rad1-Rad10. Mol. Cell. Biol. 23:2003;3487-3496.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3487-3496
    • Bastin-Shanower, S.A.1    Fricke, W.M.2    Mullen, J.R.3    Brill, S.J.4
  • 55
    • 0028808098 scopus 로고
    • Role of the Rad1 and Rad10 proteins in nucleotide excision repair and recombination
    • Davies A.A., Friedberg E.C., Tomkinson A.E., Wood R.D., West S.C. Role of the Rad1 and Rad10 proteins in nucleotide excision repair and recombination. J. Biol. Chem. 270:1995;24638-24641.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24638-24641
    • Davies, A.A.1    Friedberg, E.C.2    Tomkinson, A.E.3    Wood, R.D.4    West, S.C.5
  • 56
    • 0026498944 scopus 로고
    • Removal of nonhomologous DNA ends in double-strand break recombination: The role of the yeast ultraviolet repair gene RAD1
    • Fishman-Lobell J., Haber J.E. Removal of nonhomologous DNA ends in double-strand break recombination: the role of the yeast ultraviolet repair gene RAD1. Science. 258:1992;480-484.
    • (1992) Science , vol.258 , pp. 480-484
    • Fishman-Lobell, J.1    Haber, J.E.2
  • 57
    • 0028927573 scopus 로고
    • RAD1 and RAD10, but not other excision repair genes, are required for double-strand break-induced recombination in Saccharomyces cerevisiae
    • Ivanov E.L., Haber J.E. RAD1 and RAD10, but not other excision repair genes, are required for double-strand break-induced recombination in Saccharomyces cerevisiae. Mol. Cell. Biol. 15:1995;2245-2251.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2245-2251
    • Ivanov, E.L.1    Haber, J.E.2
  • 58
    • 0042732955 scopus 로고    scopus 로고
    • The role of yeast DNA 3′-phosphatase Tpp1 and Rad1/Rad10 endonuclease in processing spontaneous and induced base lesions
    • Karumbati A.S., Deshpandel R.A., Jilani A., Vance J.R., Ramotar D., Wilson T.E. The role of yeast DNA 3′-phosphatase Tpp1 and Rad1/Rad10 endonuclease in processing spontaneous and induced base lesions. J. Biol. Chem. 278:2003;31434-31443.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31434-31443
    • Karumbati, A.S.1    Deshpandel, R.A.2    Jilani, A.3    Vance, J.R.4    Ramotar, D.5    Wilson, T.E.6
  • 59
    • 0035355342 scopus 로고    scopus 로고
    • Silent repair accounts for cell cycle specificity in the signaling of oxidative DNA lesions
    • Leroy C., Mann C., Marsolier M.C. Silent repair accounts for cell cycle specificity in the signaling of oxidative DNA lesions. EMBO J. 20:2001;2896-2906.
    • (2001) EMBO J. , vol.20 , pp. 2896-2906
    • Leroy, C.1    Mann, C.2    Marsolier, M.C.3
  • 60
    • 0034108218 scopus 로고    scopus 로고
    • Evidence for the involvement of nucleotide excision repair in the removal of abasic sites in yeast
    • Torres-Ramos C.A., Johnson R.E., Prakash L., Prakash S. Evidence for the involvement of nucleotide excision repair in the removal of abasic sites in yeast. Mol. Cell. Biol. 20:2000;3522-3528.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3522-3528
    • Torres-Ramos, C.A.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4
  • 61
    • 0037108948 scopus 로고    scopus 로고
    • Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage
    • Vance J.R., Wilson T.E. Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage. Proc. Natl. Acad. Sci. U.S.A. 99:2002;13669-13674.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13669-13674
    • Vance, J.R.1    Wilson, T.E.2
  • 63
    • 0031889266 scopus 로고    scopus 로고
    • Synergism between yeast nucleotide and base excision repair pathways in the protection against DNA methylation damage
    • Xiao W., Chow B.L. Synergism between yeast nucleotide and base excision repair pathways in the protection against DNA methylation damage. Curr. Genet. 33:1998;92-99.
    • (1998) Curr. Genet. , vol.33 , pp. 92-99
    • Xiao, W.1    Chow, B.L.2
  • 66
    • 0035833662 scopus 로고    scopus 로고
    • DNA postreplication repair and mutagenesis in Saccharomyces cerevisiae
    • Broomfield S., Hryciw T., Xiao W. DNA postreplication repair and mutagenesis in Saccharomyces cerevisiae. Mutat. Res. 486:2001;167-184.
    • (2001) Mutat. Res. , vol.486 , pp. 167-184
    • Broomfield, S.1    Hryciw, T.2    Xiao, W.3
  • 67
    • 0033899540 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways
    • Xiao W., Chow B.L., Broomfield S., Hanna M. The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways. Genetics. 155:2000;1633-1641.
    • (2000) Genetics , vol.155 , pp. 1633-1641
    • Xiao, W.1    Chow, B.L.2    Broomfield, S.3    Hanna, M.4
  • 68
    • 0035902585 scopus 로고    scopus 로고
    • Single-strand interruptions in replicating chromosomes cause double-strand breaks
    • Kuzminov A. Single-strand interruptions in replicating chromosomes cause double-strand breaks. Proc. Natl. Acad. Sci. U.S.A. 98:2001;8241-8246.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8241-8246
    • Kuzminov, A.1
  • 69
    • 0038799991 scopus 로고    scopus 로고
    • Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae
    • Paques F., Haber J.E. Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 63:1999;349-404.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 349-404
    • Paques, F.1    Haber, J.E.2
  • 70
    • 0020488536 scopus 로고
    • Coding properties of poly(deoxycytidylic acid) templates containing uracil or apyrimidinic sites: In vitro modulation of mutagenesis by deoxyribonucleic acid repair enzymes
    • Boiteux S., Laval J. Coding properties of poly(deoxycytidylic acid) templates containing uracil or apyrimidinic sites: in vitro modulation of mutagenesis by deoxyribonucleic acid repair enzymes. Biochemistry. 21:1982;6746-6751.
    • (1982) Biochemistry , vol.21 , pp. 6746-6751
    • Boiteux, S.1    Laval, J.2
  • 71
    • 0021102422 scopus 로고
    • Insertion of nucleotides opposite apurinic/apyrimidinic sites in deoxyribonucleic acid during in vitro synthesis: Uniqueness of adenine nucleotides
    • Sagher D., Strauss B. Insertion of nucleotides opposite apurinic/apyrimidinic sites in deoxyribonucleic acid during in vitro synthesis: uniqueness of adenine nucleotides. Biochemistry. 22:1983;4518-4526.
    • (1983) Biochemistry , vol.22 , pp. 4518-4526
    • Sagher, D.1    Strauss, B.2
  • 73
    • 0028133245 scopus 로고
    • Specificity of the mutator caused by deletion of the yeast structural gene (APN1) for the major apurinic endonuclease
    • Kunz B.A., Henson E.S., Roche H., Ramotar D., Nunoshiba T., Demple B. Specificity of the mutator caused by deletion of the yeast structural gene (APN1) for the major apurinic endonuclease. Proc. Natl. Acad. Sci. U.S.A. 91:1994;8165-8169.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8165-8169
    • Kunz, B.A.1    Henson, E.S.2    Roche, H.3    Ramotar, D.4    Nunoshiba, T.5    Demple, B.6
  • 75
    • 0032518911 scopus 로고    scopus 로고
    • Release of normal bases from intact DNA by a native DNA repair enzyme
    • Berdal K.G., Johansen R.F., Seeberg E. Release of normal bases from intact DNA by a native DNA repair enzyme. EMBO J. 17:1998;363-367.
    • (1998) EMBO J. , vol.17 , pp. 363-367
    • Berdal, K.G.1    Johansen, R.F.2    Seeberg, E.3
  • 76
    • 0029100516 scopus 로고
    • Novel mutagenic properties of abasic sites in Saccharomyces cerevisiae
    • Gibbs P.E., Lawrence C.W. Novel mutagenic properties of abasic sites in Saccharomyces cerevisiae. J. Mol. Biol. 251:1995;229-236.
    • (1995) J. Mol. Biol. , vol.251 , pp. 229-236
    • Gibbs, P.E.1    Lawrence, C.W.2
  • 77
    • 0036924972 scopus 로고    scopus 로고
    • Difference between deoxyribose- and tetrahydrofuran-type abasic sites in the in vivo mutagenic response in yeast
    • Otsuka C., Sanadai S., Hata Y., Okuto H., Noskov V.N., Loakes D., Negishi K. Difference between deoxyribose- and tetrahydrofuran-type abasic sites in the in vivo mutagenic response in yeast. Nucleic Acids Res. 30:2002;5129-5135.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5129-5135
    • Otsuka, C.1    Sanadai, S.2    Hata, Y.3    Okuto, H.4    Noskov, V.N.5    Loakes, D.6    Negishi, K.7
  • 78
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl-transferase activity of yeast REV1 protein
    • Nelson J.R., Lawrence C.W., Hinkle D.C. Deoxycytidyl-transferase activity of yeast REV1 protein. Nature. 382:1996;729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 79
    • 0029952294 scopus 로고    scopus 로고
    • Thymine-thymine dimer bypass by yeast DNA polymerase zeta
    • Nelson J.R., Lawrence C.W., Hinkle D.C. Thymine-thymine dimer bypass by yeast DNA polymerase zeta. Science. 272:1996;1646-1649.
    • (1996) Science , vol.272 , pp. 1646-1649
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 80
    • 0037013287 scopus 로고    scopus 로고
    • Yeast Rev1 protein is a G template specific DNA polymerase
    • Haracska L., Prakash S., Prakash L. Yeast Rev1 protein is a G template specific DNA polymerase. J. Biol. Chem. 277:2002;15546-15551.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15546-15551
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 81
    • 0032584658 scopus 로고    scopus 로고
    • Characterization of the two small subunits of Saccharomyces cerevisiae DNA polymerase delta
    • Gerik K.J., Li X., Pautz A., Burgers P.M. Characterization of the two small subunits of Saccharomyces cerevisiae DNA polymerase delta. J. Biol. Chem. 273:1998;19747-19755.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19747-19755
    • Gerik, K.J.1    Li, X.2    Pautz, A.3    Burgers, P.M.4
  • 82
  • 83
    • 0034852569 scopus 로고    scopus 로고
    • Interaction with PCNA is essential for yeast DNA polymerase η function
    • Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L. Interaction with PCNA is essential for yeast DNA polymerase η function. Mol. Cell. 8:2001;407-415.
    • (2001) Mol. Cell , vol.8 , pp. 407-415
    • Haracska, L.1    Kondratick, C.M.2    Unk, I.3    Prakash, S.4    Prakash, L.5
  • 85
    • 0242412184 scopus 로고    scopus 로고
    • Origin of endogenous DNA abasic sites in Saccharomyces cerevisiae
    • Guillet M., Boiteux S. Origin of endogenous DNA abasic sites in Saccharomyces cerevisiae. Mol. Cell. Biol. 23:2003;8386-8394.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8386-8394
    • Guillet, M.1    Boiteux, S.2
  • 86
    • 0023712476 scopus 로고
    • The RAD9 gene controls the cell cycle response to DNA damage in Saccharomyces cerevisiae
    • Weinert T.A., Hartwell L.H. The RAD9 gene controls the cell cycle response to DNA damage in Saccharomyces cerevisiae. Science. 241:1988;317-322.
    • (1988) Science , vol.241 , pp. 317-322
    • Weinert, T.A.1    Hartwell, L.H.2
  • 87
    • 0037178748 scopus 로고    scopus 로고
    • Interfaces between the detection, signaling, and repair of DNA damage
    • Rouse J., Jackson S.P. Interfaces between the detection, signaling, and repair of DNA damage. Science. 297:2002;547-551.
    • (2002) Science , vol.297 , pp. 547-551
    • Rouse, J.1    Jackson, S.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.