Crosstalk of DNA glycosylases with pathways other than base excision repair

DNA Repair

Volumn 6, Issue 4, 2007, Pages 517-529

  Kovtun, Irina V ^a   McMurray, Cynthia T ^a  

^a MAYO GRADUATE SCHOOL   (United States)

Author keywords

Base excision repair; Crosstalk; Glycosylase; Mismatch repair; Transcription

Indexed keywords

DNA GLYCOSYLTRANSFERASE;

ARTICLE; DNA DAMAGE; DNA METHYLATION; DNA REPAIR; DNA TRANSCRIPTION; ENZYME ACTIVITY; EXCISION REPAIR; MISMATCH REPAIR; PRIORITY JOURNAL;

ANIMALS; DNA DAMAGE; DNA GLYCOSYLASES; DNA MISMATCH REPAIR; DNA REPAIR; DNA REPAIR ENZYMES; MICE; NUCLEOTIDES; OXIDATION-REDUCTION; TRANSCRIPTION, GENETIC;

EID: 33847673066     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2006.10.015     Document Type: Article

References (108)

1. Friedberg E.C., Walker G.C., and Siede W. DNA Repair and Mutagenesis (1995), American Society for Microbiology Press, Washington, DC
2. Lindahl T. Suppression of spontaneous mutagenesis in human cells by DNA base excision-repair. Mutat. Res. 462 (2000) 129-135
3. Izumi T., Wiederhold L.R., Roy G., Roy R., Jaiswal A., Bhakat K.K., Mitra S., and Hazra T.K. Mammalian DNA base excision repair proteins: their interactions and role in repair of oxidative DNA damage. Toxicology 193 (2003) 43-65
4. Slupphaug G., Kavli B., and Krokan H.E. The interacting pathways for prevention and repair of oxidative DNA damage. Mutat. Res. 531 (2003) 231-251
5. Adelman R., Saul R.L., and Ames B.N. Oxidative damage to DNA: relation to species metabolic rate and life span. Proc. Natl. Acad. Sci. USA 85 (1988) 2706-2708
6. Ames B.N., Shigenaga M.K., and Hagen T.M. Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. USA 90 (1993) 7915-7922
7. Finkel T., and Holbrook N.J. Oxidants, oxidative stress and the biology of ageing. Nature 408 (2000) 239-247
8. Earley M.C., and Crouse G.F. The role of mismatch repair in the prevention of base pair mutations in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. 95 (1998) 15487-15491
9. Cadet J., Berger M., Douki T., and Ravanat J.L. Oxidative damage to DNA: formation, measurement, and biological significance. Rev. Physiol. Biochem. Pharmacol. 131 (1997) 1-87
10. DeWeese T.L., Shipman J.M., Larrier N.A., Kidd N.M.L.R., Groopman J.D., Cutler R.G., te Riele H., and Nelson W.G. Mouse embryonic stem cells carrying one or two defective Msh2 alleles respond abnormally to oxidative stress inflicted by low-level radiation. Proc. Natl. Acad. Sci. USA 95 (1998) 11915-11920
11. Ni T.T., Marsischky G.T., and Kolodner R.D. MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae. Mol. Cell 4 (1999) 439-444
12. Michaels M.L., Tchou J., Grollman A.P., and Miller J.H. A repair system for 8-oxo-7,8-dihydrodeoxyguanine. Biochemistry 31 (1992) 10964-10968
13. Wyrzykowski J., and Volkert M.R. The Escherichia coli methyl-directed mismatch repair system repairs base pairs containing oxidative lesions. J. Bacteriol. 185 (2003) 1701-1704
14. Zhao J., and Winkler M.E. Reduction of GC ->TA transversion mutation by overexpression of MutS in Escherichia coli K-12. J. Bacteriol. 182 (2000) 5025-5028
15. Klungland A., Rosewell I., Hollenbach S., Larsen E., Daly G., Epe B., Seeberg E., Lindahl T., and Barnes D.E. Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage. Proc. Natl. Acad. Sci. USA 96 (1999) 13300-13305
16. Minowa O., Arai T., Hirano M., Monden Y., Nakai S., Fukuda M., Itoh M., Takano H., Hippou Y., Aburatani H., Masumura K., Nohmi T., Nishimura S., and Noda T. Mmh/Ogg1 gene inactivation results in accumulation of 8-hydroxyguanine in mice. Proc. Natl. Acad. Sci. USA 97 (2000) 4156-4161
17. Colussi C., Parlanti E., Degan P., Aquilina G., Barnes D., Macpherson P., Karran P., Crescenzi M., Dogliotti E., and Bignami M. The mammalian mismatch repair pathway removes DNA 8-oxodGMP incorporated from the oxidized dNTP pool. Curr. Biol. 12 (2002) 912-918
18. Mazurek A., Berardini M., and Fishel R. Activation of human MutS homologs by 8-oxo-guanine DNA damage. J. Biol. Chem. 277 (2002) 8260-8266
19. Larson E.D., Iams K., and Drummond J.T. Strand-specific processing of 8-oxoguanine by the human mismatch repair pathway: inefficient removal of 8-oxoguanine paired with adenine or cytosine. DNA Repair 2 (2003) 1199-1210
20. Shibutani S., Bodepudi V., Johnson F., and Grollman A.P. Translesional synthesis on DNA templates containing 8-oxo-7,8-dihydrodeoxyadenosine. Biochemistry 32 (1993) 4615-4621
21. Bertrand P., Tishkoff D.X., Filosi N., Dasgupta R., and Kolodner R.D. Physical interaction between components of DNA mismatch repair and nucleotide excision repair. Proc. Natl. Acad. Sci. USA 95 (1998) 14278-14283
22. Gu Y., Parker A., Wilson T.M., Bai H., Chang D.Y., and Lu A.L. Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6. J. Biol. Chem. 277 (2002) 11135-11142
23. Eide L., Bjoras M., Pirovano M., Alseth I., Berdal K.G., and Seeberg E. 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 (1996) 10735-10740
24. Alseth I., Eide L., Pirovano M., Rognes T., Seeberg E., and 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
25. You H.J., Swanson R.L., Harrington C., Corbett A.H., Jinks-Robertson S., Senturker S., Wallace S.S., Boiteux S., Dizdaroglu M., and Doetsch P.W. Saccharomyces cerevisiae Ntg1p and Ntg2p: broad specificity N-glycosylases for the repair of oxidative DNA damage in the nucleus and mitochondria. Biochemistry 38 (1999) 11298-11306
26. Swanson R.L., Morey N.J., Doetsch P.W., and 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
27. Gellon L., Barbey R., Auffret van der Kemp P., Thomas D., and Boiteux S. Synergism between base excision repair, mediated by the DNA glycosylases Ntg1 and Ntg2, and nucleotide excision repair in the removal of oxidatively damaged DNA bases in Saccharomyces cerevisiae. Mol. Genet. Genomics 265 (2001) 1087-1096
28. Gellon L., Werner M., and Boiteux S. Ntg2p, a Saccharomyces cerevisiae DNA N-glycosylase/apurinic or apyrimidinic lyase involved in base excision repair of oxidative DNA damage, interacts with the DNA mismatch repair protein Mlh1p. Identification of a Mlh1p binding motif. J. Biol. Chem. 277 (2002) 29963-29972
29. Senturker S., Auffret van der Kemp P., You H.J., Doetsch P.W., Dizdaroglu M., and 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
30. Augeri L., Lee Y.M., Barton A.B., and Doetsch P.W. Purification, characterization, gene cloning, and expression of Saccharomyces cerevisiae redoxyendonuclease, a homolog of Escherichia coli endonuclease III. Biochemistry 36 (1997) 721-729
31. Malyarchuk S., Brame K.L., Youngblood R., Shi R., and Harrison L. Two clustered 8-oxo-7,8-dihydroguanine (8-oxodG) lesions increase the point mutation frequency of 8-oxodG, but do not result in double strand breaks or deletions in Escherichia coli. Nucleic Acids Res. 32 (2004) 5721-5731
32. Budworth H., and Dianov G.L. Mode of inhibition of short-patch base excision repair by thymine glycol within clustered DNA lesions. J. Biol. Chem. 278 (2003) 9378-9381
33. Eot-Houllier G., Eon-Marchais S., Gasparutto D., and Sage E. Processing of a complex multiply damaged DNA site by human cell extracts and purified repair proteins. Nucleic Acids Res. 33 (2005) 260-271
34. Kat A., Thilly W.G., Fang W.H., Longley M.J., Li G.M., and Modrich P. An alkylation-tolerant, mutator human cell line is deficient in strand-specific mismatch repair. Proc. Natl. Acad. Sci. USA 90 (1993) 6424-6428
35. Duckett D.R., Drummond J.T., Murchie A.I., Reardon J.T., Sancar A., Lilley D.M., and Modrich P. Human MutSalpha recognizes damaged DNA base pairs containing O6-methylguanine, O4-methylthymine, or the cisplatin-d (GpG) adduct. Proc. Natl. Acad. Sci. USA 93 (1996) 6443-6447
36. Mironov N.M., Bleicher F., Martel-Planche G., and Montesano R. Nonrandom distribution of O6-methylguanine in H-ras gene sequence from DNA modified with N-methyl-N-nitrosourea. Mutat. Res. 288 (1993) 197-205
37. Bartolomei M.S., and Tilghman S.M. Genomic imprinting in mammals. Annu. Rev. Genet. 31 (1997) 493-525
38. Karran P., and Bignami M. In: Smith P.J., and Jones C.J. (Eds). DNA Recombination and Repair (1999), Oxford University Press, New York 66-159
39. Krawczak M., Ball E.V., and Cooper D.N. Neighboring-nucleotide effects on the rates of germ-line single-base-pair substitution in human genes. Am. J. Hum. Genet. 63 (1998) 474-488
40. Jaenisch R., and Bird A. Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals. Nat. Genet. 33 (2003) 245-254
41. Lindahl T. An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues. Proc. Natl Acad. Sci. USA 71 (1974) 3649-3653
42. Ehrlich M., Norris K.F., Wang R.Y., Kuo K.C., and Gehrke C.W. DNA cytosine methylation and heat-induced deamination. Biosci. Rep. 6 (1986) 387-393
43. Griffin S., Branch P., Xu Y.Z., and Karran P. DNA mismatch binding and incision at modified guanine bases by extracts of mammalian cells: implications for tolerance to DNA methylation damage. Biochemistry 33 (1994) 4787-4793
44. De Vita V.T., Hellmann S., and Rosenberg S.A. Cancer, Principles and Practice of Oncology (2001), Lippincott-Raven, Philadelphia
45. Yoshioka K., Yoshioka Y., and Hsieh P. ATR kinase activation mediated by MutSalpha and MutLalpha in response to cytotoxic O6-methylguanine adducts. Mol. Cell. 22 (2006) 501-510
46. Hardeland U., Bentele M., Lettieri T., Steinacher R., Jiricny J., and Schar P. Thymine DNA glycosylase. Prog. Nucleic Acid Res. Mol. Biol. 68 (2001) 235-253
47. Neddermann P., and Jiricny J. Efficient removal of uracil from G.U mispairs by the mismatch-specific thymine DNA glycosylase from HeLa cells. Proc. Natl. Acad. Sci. USA 91 (1994) 1642-1646
48. Barrett T.E., Savva R., Panayotou G., Barlow T., Brown T., Jiricny J., and Pearl L.H. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92 (1998) 117-129
49. Barrett T.E., Savva R., Barlow T., Brown T., Jiricny J., and Pearl L.H. Structure of a DNA base-excision product resembling a cisplatin inter-strand adduct. Nat. Struct. Biol. 5 (1998) 697-701
50. Barrett T.E., Scharer O.D., Savva R., Brown T., Verdine G.L., and Pear L.H. Crystal structure of a thwarted mismatch glycosylase DNA repair complex. EMBO J. 18 (1999) 6599-6609
51. Waters T.R., and Swann P.F. Kinetics of the action of thymine DNA glycosylase. J. Biol. Chem. 273 (1998) 20007-20014
52. Waters T.R., Gallinari P., Jiricny J., and Swann P.F. Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1. J. Biol. Chem. 274 (1999) 267-274
53. Waters T.R., and Swann P.F. Thymine-DNA glycosylase and G to A transition mutations at CpG sites. Mutat. Res. 462 (2000) 137-147
54. Nedderman P., Gallinari P., Lettieri T., Schmid D., Truong O., Hsuan J.J., Wiebauer K., and Jiricny J. Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. J. Biol. Chem. 271 (1996) 12767-12774
55. Batty D., Rapic'-Otrin V., Levine A.S., and Wood R.D. Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. J. Mol. Biol. 300 (2000) 275-290
56. Kusumoto R., Masutani C., Sugasawa K., Iwai S., Araki M., Uchida A., Mizukoshi T., and Hanaoka F. Diversity of the damage recognition step in the global genomic nucleotide excision repair in vitro. Mutat. Res. 485 (2001) 219-227
57. Sugasawa K., Shimizu Y., Iwai S., and Hanaoka F. A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex. DNA Repair 1 (2002) 95-107
58. Shimizu Y., Iwai S., Hanaoka F., and Sugasawa K. Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase. EMBO J. 22 (2003) 164-173
59. Fujiwara Y., Masutani C., Mizukoshi T., Kondo J., Hanaoka F., and Iwai S. Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J. Biol. Chem. 274 (1999) 20027-20033
60. Hendrich B., and Bird A. Identification and characterization of a family of mammalian methyl-CpG binding proteins. Mol. Cell. Biol. 18 (1998) 6538-6547
61. Bellacosa A., Cicchillitti L., Schepis F., Riccio A., Yeung A.T., Matsumoto Y., Golemis E.A., Genuardi M., and Neri G. MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1. Proc. Natl. Acad. Sci. USA 96 (1999) 3969-3974
62. Hendrich B., Hardeland U., Ng H.H., Jiricny J., and Bird A. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature 401 (1999) 301-304
63. Cortellino S., Turner D., Masciullo V., Schepis F., Albino D., Daniel R., Skalka A.M., Meropol N.J., Alberti C., Larue L., and Bellacosa A. The base excision repair enzyme MED1 mediates DNA damage response to antitumor drugs and is associated with mismatch repair system integrity. Proc. Natl. Acad. Sci. USA 100 (2003) 15071-15076
64. Millar C.B., Guy J., Sansom O.J., Selfridge J., MacDougall E., Hendrich B., Keightley P.D., Bishop S.M., Clarke A.R., and Bird A. Enhanced CpG mutability and tumorigenesis in MBD4-deficient mice. Science 297 (2002) 403-405
65. Bader S., Walker M., Hendrich B., Bird A., Bird C., Hooper M., and Wyllie A. Somatic frameshift mutations in the MBD4 gene of sporadic colon cancers with mismatch repair deficiency. Oncogene 18 (1999) 8044-8047
66. Bader S., Walker M., and Harrison D. Most microsatellite unstable sporadic colorectal carcinomas carry MBD4 mutations. Br. J. Cancer 83 (2000) 1646-1649
67. Sansom O.J., Bishop S.M., Bird A., and Clarke A.R. MBD4 deficiency does not increase mutation or accelerate tumorigenesis in mice lacking MMR. Oncogene 23 (2004) 5693-5696
68. Sansom O.J., Zabkiewicz J., Bisho S.M., Guy J., Bird A., and Clarke A.R. MBD4 deficiency reduces the apoptotic response to DNA-damaging agents in the murine small intestine. Oncogene 22 (2003) 7130-7136
69. Sansom O.J., Bishop S.M., Court H., Dudley S., Liskay R.M., and Clarke A.R. Apoptosis and mutation in the murine small intestine: loss of Mlh1- and Pms2-dependent apoptosis leads to increased mutation in vivo. DNA Repair 2 (2003) 1029-1039
70. Rada C., Williams G.T., Nilsen H., Barnes D.E., Lindahl T., and Neuberger M.S. Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice. Curr. Biol. 12 (2002) 1748-1755
71. Rada C., Di Noia J.M., and Neuberger M.S. Mismatch recognition and uracil excision provide complementary paths to both Ig switching and the A/T-focused phase of somatic mutation. Mol. Cell 16 (2004) 163-171
72. Imai K., Slupphaug G., Lee W.I., Revy P., Nonoyama S., Catalan N., Yel L., Forveille M., Kavli B., Krokan H.E., Ochs H.D., Fischer A., and Durandy A. Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination. Nat. Immunol. 4 (2003) 1023-1028
73. Begum N.A., Kinoshita K., Kakazu N., Muramatsu M., Nagaoka H., Shinkura R., Biniszkiewicz D., Boyer L.A., Jaenisch R., and Honjo T. Uracil DNA glycosylase activity is dispensable for immunoglobulin class switch. Science 20 305 (2004) 1160-1163
74. Li Z., Scherer S.J., Ronai D., Iglesias-Ussel M.D., Peled J.U., Bardwell P.D., Zhuang M., Lee K., Martin A., Edelmann W., and Scharff M.D. Examination of Msh6- and Msh3-deficient mice in class switching reveals overlapping and distinct roles of MutS homologues in antibody diversification. J. Exp. Med. 200 (2004) 47-59
75. Martomo S.A., Yang W.W., and Gearhar P.J. A role for Msh6 but not Msh3 in somatic hypermutation and class switch recombination. J. Exp. Med. 200 (2004) 61-68
76. Larson E.D., Duquette M.L., Cummings W.J., Streiff R.J., and Maizels N. MutS alpha binds to and promotes synapsis of transcriptionally activated immunoglobulin switch regions. Curr. Biol. 15 (2005) 470-474
77. Li Z., Zhao C., Iglesias-Ussel M.D., Polonskaya Z., Zhuang M., Yang G., Luo Z., Edelmann W., and Scharff M.D. The mismatch repair protein Msh6 influences the in vivo AID targeting to the Ig locus. Immunity 24 (2006) 393-403
78. Larson E.D., Cummings W.J., Bednarski D.W., and Maizels N. MRE11/RAD50 cleaves DNA in the AID/UNG-dependent pathway of immunoglobulin gene diversification. Mol. Cell 20 (2005) 367-375
79. Tini M., Benecke A., Um S.J., Torchia J., Evans R.M., and Chambon P. Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol. Cell 9 (2002) 265-277
80. Chen D., Lucey M.J., Phoenix F., Lopez-Garcia J., Hart S.M., Losson R., Buluwela L., Coombes R.C., Chambon P., Schar P., and Ali S. T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha. J. Biol. Chem. 278 (2003) 38586-38592
81. Lucey M.J., Chen D., Lopez-Garcia J., Hart S.M., Phoenix F., Al-Jehani R., Alao J.P., White R., Kindle K.B., Losson R., Chambon P., Parker M.G., Schar P., Heery D.M., Buluwela L., and Ali S. T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif. Nucleic Acids Res. 33 (2005) 6393-6404
82. Missero C., Pirro M.T., Simeone S., Pischetola M., and Di Lauro R. The DNA glycosylase T:G mismatch-specific thymine DNA glycosylase represses thyroid transcription factor-1-activated transcription. J. Biol. Chem. 276 (2001) 33569-33575
83. Likhite V.S., Cass E.I., Anderson S.D., Yates J.R., and Nardulli A.M. Interaction of estrogen receptor alpha with 3-methyladenine DNA glycosylase modulates transcription and DNA repair. J. Biol. Chem. 279 (2004) 16875-16882
84. Wyatt M.D., Allan J.M., Lau A.Y., Ellenberger T.E., and Samson L.D. 3-methyladenine DNA glycosylases: structure, function, and biological importance. Bioessays (1999) 21668-21676
85. Hurley L.H. DNA and its associated processes as targets for cancer therapy. Nat. Rev. Cancer (2002) 2188-2200
86. Engelward B.P., Weeda G., Wyatt M.D., Broekhof J.L., de Wit J., Donker I., Allan J.M., Gold B., Hoeijmakers J.H., and Samson L.D. Base excision repair deficient mice lacking the Aag alkyladenine DNA glycosylase. Proc. Natl. Acad. Sci. USA 84 (1997) 13087-13092
87. Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M., Kawasuji M., and Nakao M. Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin. Proc. Natl. Acad. Sci. USA 100 (2003) 12859-12864
88. Kondo E., Gu Z., Horii A., and Fukushige S. The thymine DNA glycosylase MBD4 represses transcription and is associated with methylated p16 (INK4a) and hMLH1 genes. Mol. Cell. Biol. 25 (2005) 4388-4396
89. Lehmann A.R. DNA repair-deficient diseases, xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy. Biochimie 85 (2003) 1101-1111
90. Cleaver J.E. Cancer in Xeroderma Pigmentosum and related disorders of DNA repair. Nat. Rev. Cancer 5 (2005) 564-573
91. Friedberg E.C. DNA damage and repair. Nature 421 (2003) 436-440
92. Hanawalt P.C., Ford J.M., and Lloyd D.R. Functional characterization of global genomic DNA repair and its implications for cancer. Mutat. Res. 544 (2003) 107-114
93. Bradsher J., Auriol J., Proietti de Santis L., Iben S., Vonesch J.L., Grummt I., and Egly J.M. CSB is a component of RNA pol I transcription. Mol. Cell 10 (2002) 819-829
94. an Gool Va.J., Citterio E., Rademakers S., van Os R., Vermeulen W., Constantinou A., Egly J.M., Bootsma D., and Hoeijmakers J.H. The Cockayne syndrome B protein, involved in transcription-coupled DNA repair, resides in an RNA polymerase II-containing complex. EMBO J. 16 (1997) 5955-5965
95. Hosfield D.J., Daniels D.S., Mol C.D., Putnam C.D., Parikh S.S., and Tainer J.A. DNA damage recognition and repair pathway coordination revealed by the structural biochemistry of DNA repair enzymes. Prog. Nucleic Acid Res. Mol. Biol. 68 (2001) 315-347
96. Reardon J.T., Bessho T., Kung H.C., Bolton P.H., and Sancar A. In vitro repair of oxidative DNA damage by human nucleotide excision repair system: possible explanation for neurodegeneration in xeroderma pigmentosum patients. Proc. Natl. Acad. Sci. USA 94 (1997) 9463-9468
97. Kisby G.E., Lesselroth H., Olivas A., Samson L., Gold B., Tanaka K., and Turker M.S. Role of nucleotide- and base-excision repair in genotoxin-induced neuronal cell death. DNA Repair 6 (2004) 617-627
98. Wood R.D. DNA damage recognition during nucleotide excision repair in mammalian cells. Biochimie 81 (1999) 39-44
99. Hohl M., Thorel F., Clarkson S.G., and Schärer O.D. Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG. J. Biol. Chem. 278 (2003) 19500-19508
100. Constantinou A., Gunz D., Evans E., Lalle P., Bates P.A., Wood R.D., and Clarkson S.G. Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair. J. Biol. Chem. 274 (1999) 5637-5648
101. Viswanathan A., and Doetsch P.W. Effects of nonbulky DNA base damages on Escherichia coli RNA polymerase-mediated elongation and promoter clearance. J. Biol. Chem. 273 (1998) 21276-21281
102. Tornaletti S., Maeda L.S., Lloyd D.R., Reines D., and Hanawalt P.C. Effect of thymine glycol on transcription elongation by T7 RNA polymerase and mammalian RNA polymerase II. J. Biol. Chem. 276 (2001) 45367-45371
103. Bessho T. Nucleotide excision repair 3′ endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase. Nucleic Acids Res. 27 (1999) 979-983
104. Klungland A., Hoss M., Gunz D., Constantinou A., Clarkson S.G., Doetsch P.W., Bolton P.H., Wood R.D., and Lindahl T. Base excision repair of oxidative DNA damage activated by XPG protein. Mol. Cell. 3 (1999) 33-42
105. Plosky B., Samson L., Engelward B.P., Gold B., Schlaen B., Millas T., Magnotti M., Schor Jl J., and Scicchitano D.A. Base excision repair and nucleotide excision repair contribute to the removal of N-methylpurines from active genes. DNA Repair 8 (2002) 683-696
106. Bregeon D., Doddridge Z.A., You H.J., Weiss B., and Doetsch P.W. Transcriptional mutagenesis induced by uracil and 8-oxoguanine in Escherichia coli. Mol Cell 12 (2003) 959-970
107. Shah D., Kelly J., Zhang Y., Dande P., Martinez J., Ortiz G., Fronz G., Tran H., Soto A.M., Marky L., and Gold B. Evidence in Escherichia coli that N3-methyladenine lesions induced by a minor groove binding methyl sulfonate ester can be processed by both base and nucleotide excision repair. Biochemistry 40 (2001) 1796-1803
108. Miao F., Bouziane M., Dammann R., Masutani C., Hanaoka F., Pfeifer G., and O'Connor T.R. 3-Methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteins. J. Biol. Chem. 275 (2000) 28433-28438