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Volumn 456, Issue 1, 2013, Pages 89-98

Histone deacetylase SIRT1 modulates and deacetylates DNA base excision repair enzyme thymine DNA glycosylase

Author keywords

5 fluorouracil; Acetylation; Base excision repair; Deacetylase; DNA repair; SIRT1; Thymine DNA glycosylase (TDG)

Indexed keywords

5 CARBOXYLCYTOSINE; 5 FORMYLCYTOSINE; CYTOSINE DERIVATIVE; DNA BASE; FLUOROURACIL; SIRTUIN 1; THYMINE DNA GLYCOSYLASE; UNCLASSIFIED DRUG;

EID: 84886551415     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130670     Document Type: Article
Times cited : (27)

References (51)
  • 1
    • 0034733899 scopus 로고    scopus 로고
    • Base excision repair of DNA in mammalian cells
    • DOI 10.1016/S0014-5793(00)01674-4, PII S0014579300016744
    • Krokan, H. E., Nilsen, H., Skorpen, F., Otterlei, M. and Slupphaug, G. (2000) Base excision repair of DNA in mammalian cells. FEBS Lett. 476, 73-77 (Pubitemid 30394654)
    • (2000) FEBS Letters , vol.476 , Issue.1-2 , pp. 73-77
    • Krokan, H.E.1    Nilsen, H.2    Skorpen, F.3    Otterlei, M.4    Slupphaug, G.5
  • 2
    • 33847663262 scopus 로고    scopus 로고
    • The enigmatic thymine DNA glycosylase
    • DOI 10.1016/j.dnarep.2006.10.013, PII S1568786406003223, Repair of small base lesions in DNA-from molecular biology to phenotype
    • Cortazar, D., Kunz, C., Saito, Y., Steinacher, R. and Schar, P. (2007) The enigmatic thymine DNA glycosylase. DNA Repair 6, 489-504 (Pubitemid 46357052)
    • (2007) DNA Repair , vol.6 , Issue.4 , pp. 489-504
    • Cortazar, D.1    Kunz, C.2    Saito, Y.3    Steinacher, R.4    Schar, P.5
  • 5
    • 0038074420 scopus 로고    scopus 로고
    • The versatile thymine DNA-glycosylase: A comparative characterization of the human, Drosophila and fission yeast orthologs
    • DOI 10.1093/nar/gkg344
    • Hardeland, U., Bentele, M., Jiricny, J. and Schar, P. (2003) The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs. Nucleic Acids Res. 31, 2261-2271 (Pubitemid 37442093)
    • (2003) Nucleic Acids Research , vol.31 , Issue.9 , pp. 2261-2271
    • Hardeland, U.1    Bentele, M.2    Jiricny, J.3    Schar, P.4
  • 6
    • 34948854919 scopus 로고    scopus 로고
    • Excision of 5-halogenated uracils by human thymine DNA glycosylase: Robust activity for DNA contexts other than CpG
    • DOI 10.1074/jbc.M704253200
    • Morgan, M. T., Bennett, M. T. and Drohat, A. C. (2007) Excision of 5-halogenated uracils by human thymine DNA glycosylase. Robust activity for DNA contexts other than CpG. J. Biol. Chem. 282, 27578-27586 (Pubitemid 47529476)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.38 , pp. 27578-27586
    • Morgan, M.T.1    Bennett, M.T.2    Drohat, A.C.3
  • 7
    • 0023853921 scopus 로고
    • The CpG dinucleotide and human genetic disease
    • Cooper, D. N. and Youssoufian, H. (1988) The CpG dinucleotide and human genetic disease. Hum. Genet. 78, 151-155 (Pubitemid 18069872)
    • (1988) Human Genetics , vol.78 , Issue.2 , pp. 151-155
    • Cooper, D.N.1    Youssoufian, H.2
  • 8
    • 43049105333 scopus 로고    scopus 로고
    • Demethylation of (cytosine-5-C-methyl) DNA and regulation of transcription in the epigenetic pathways of cancer development
    • Patra, S. K., Patra, A., Rizzi, F., Ghosh, T. C. and Bettuzzi, S. (2008) Demethylation of (cytosine-5-C-methyl) DNA and regulation of transcription in the epigenetic pathways of cancer development. Cancer Metastasis Rev. 27, 315-334
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 315-334
    • Patra, S.K.1    Patra, A.2    Rizzi, F.3    Ghosh, T.C.4    Bettuzzi, S.5
  • 11
    • 80052933429 scopus 로고    scopus 로고
    • DNA demethylation dynamics
    • Bhutani, N., Burns, D. M. and Blau, H. M. (2011) DNA demethylation dynamics. Cell 146, 866-872
    • (2011) Cell , vol.146 , pp. 866-872
    • Bhutani, N.1    Burns, D.M.2    Blau, H.M.3
  • 12
    • 79955538247 scopus 로고    scopus 로고
    • Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain
    • Guo, J. U., Su, Y., Zhong, C., Ming, G. L. and Song, H. (2011) Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain. Cell 145, 423-434
    • (2011) Cell , vol.145 , pp. 423-434
    • Guo, J.U.1    Su, Y.2    Zhong, C.3    Ming, G.L.4    Song, H.5
  • 13
    • 80052495940 scopus 로고    scopus 로고
    • Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA
    • He, Y. F., Li, B. Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L. et al. (2011) Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA. Science 333, 1303-1307
    • (2011) Science , vol.333 , pp. 1303-1307
    • He, Y.F.1    Li, B.Z.2    Li, Z.3    Liu, P.4    Wang, Y.5    Tang, Q.6    Ding, J.7    Jia, Y.8    Chen, Z.9    Li, L.10
  • 15
    • 77956095231 scopus 로고    scopus 로고
    • Active DNA demethylation: Many roads lead to Rome
    • Wu, S. C. and Zhang, Y. (2010) Active DNA demethylation: many roads lead to Rome. Nat. Rev. Mol. Cell Biol. 11, 607-620
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 607-620
    • Wu, S.C.1    Zhang, Y.2
  • 16
    • 80053917872 scopus 로고    scopus 로고
    • Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: Potential implications for active demethylation of CpG sites
    • Maiti, A. and Drohat, A. C. (2011) Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites. J. Biol. Chem. 286, 35334-35338
    • (2011) J. Biol. Chem , vol.286 , pp. 35334-35338
    • Maiti, A.1    Drohat, A.C.2
  • 17
    • 0035161816 scopus 로고    scopus 로고
    • Functional interactions and signaling properties of mammalian DNA mismatch repair proteins
    • DOI 10.1038/sj.cdd.4400948
    • Bellacosa, A. (2001) Functional interactions and signaling properties of mammalian DNA mismatch repair proteins. Cell Death. Differ. 8, 1076-1092 (Pubitemid 33061825)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.11 , pp. 1076-1092
    • Bellacosa, A.1
  • 18
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • DOI 10.1016/S1097-2765(02)00453-7
    • Tini, M., Benecke, A., Um, S. J., Torchia, J., Evans, R. M. and Chambon, P. (2002) Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol. Cell 9, 265-277 (Pubitemid 34195553)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.-J.3    Torchia, J.4    Evans, R.M.5    Chambon, P.6
  • 19
    • 35549003626 scopus 로고    scopus 로고
    • The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase
    • DOI 10.1093/nar/gkm678
    • Guan, X., Madabushi, A., Chang, D.-Y., Fitzgerald, M. E., Shi, G., Drohat, A. C. and Lu, A-L. (2007) The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase. Nucleic Acids Res. 35, 6207-6218 (Pubitemid 350018582)
    • (2007) Nucleic Acids Research , vol.35 , Issue.18 , pp. 6207-6218
    • Guan, X.1    Madabushi, A.2    Chang, D.-Y.3    Fitzgerald, M.E.4    Shi, G.5    Drohat, A.C.6    Lu, A.-L.7
  • 20
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation
    • Steinacher, R. and Schar, P. (2005) Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr. Biol. 15, 616-623
    • (2005) Curr. Biol , vol.15 , pp. 616-623
    • Steinacher, R.1    Schar, P.2
  • 21
    • 77950347722 scopus 로고    scopus 로고
    • Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase
    • Mohan, R. D., Litchfield, D. W., Torchia, J. and Tini, M. (2010) Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase. Nucleic Acids Res. 38, 1135-1148
    • (2010) Nucleic Acids Res , vol.38 , pp. 1135-1148
    • Mohan, R.D.1    Litchfield, D.W.2    Torchia, J.3    Tini, M.4
  • 22
  • 23
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • DOI 10.1146/annurev.biochem.73.011303.073651
    • Blander, G. and Guarente, L. (2004) The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73, 417-435 (Pubitemid 39050375)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 24
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • DOI 10.1042/BJ20070140
    • Michan, S. and Sinclair, D. (2007) Sirtuins in mammals: insights into their biological function. Biochem. J. 404, 1-13 (Pubitemid 46788079)
    • (2007) Biochemical Journal , vol.404 , Issue.1 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 27
    • 77952876986 scopus 로고    scopus 로고
    • Protein deacetylation by SIRT1: An emerging key post-translational modification in metabolic regulation
    • Yu, J. and Auwerx, J. (2010) Protein deacetylation by SIRT1: an emerging key post-translational modification in metabolic regulation. Pharmacol. Res. 62, 35-41
    • (2010) Pharmacol. Res , vol.62 , pp. 35-41
    • Yu, J.1    Auwerx, J.2
  • 28
    • 34250897968 scopus 로고    scopus 로고
    • SIRT1 regulates the function of the nijmegen breakage syndrome protein
    • DOI 10.1016/j.molcel.2007.05.029, PII S1097276507003309
    • Yuan, Z., Zhang, X., Sengupta, N., Lane, W. S. and Seto, E. (2007) SIRT1 regulates the function of the Nijmegen breakage syndrome protein. Mol. Cell 27, 149-162 (Pubitemid 46991383)
    • (2007) Molecular Cell , vol.27 , Issue.1 , pp. 149-162
    • Yuan, Z.1    Zhang, X.2    Sengupta, N.3    Lane, W.S.4    Seto, E.5
  • 32
    • 62749133315 scopus 로고    scopus 로고
    • SIRT1, is it a tumor promoter or tumor suppressor?
    • Deng, C. X. (2009) SIRT1, is it a tumor promoter or tumor suppressor? Int. J. Biol. Sci. 5, 147-152
    • (2009) Int. J. Biol. Sci , vol.5 , pp. 147-152
    • Deng, C.X.1
  • 33
    • 79955469653 scopus 로고    scopus 로고
    • Sirtuin 1 in malignant transformation: Friend or foe?
    • Fang, Y. and Nicholl, M. B. (2011) Sirtuin 1 in malignant transformation: friend or foe? Cancer Lett. 306, 10-14
    • (2011) Cancer Lett , vol.306 , pp. 10-14
    • Fang, Y.1    Nicholl, M.B.2
  • 35
    • 0028825742 scopus 로고
    • DNA determinants and substrate specificities of Escherichia coliMutY
    • Lu, A-L., Tsai-Wu, J.-J. and Cillo, J. (1995) DNA determinants and substrate specificities of Escherichia coliMutY. J. Biol. Chem. 270, 23582-23588
    • (1995) J. Biol. Chem , vol.270 , pp. 23582-23588
    • Lu, A.-L.1    Tsai-Wu, J.-J.2    Cillo, J.3
  • 37
    • 57749097697 scopus 로고    scopus 로고
    • Coordinating the initial steps of base excision repair. Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex
    • Fitzgerald, M. E. and Drohat, A. C. (2008) Coordinating the initial steps of base excision repair. Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex. J. Biol. Chem. 283, 32680-32690
    • (2008) J. Biol. Chem , vol.283 , pp. 32680-32690
    • Fitzgerald, M.E.1    Drohat, A.C.2
  • 38
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1
    • DOI 10.1074/jbc.274.1.67
    • Waters, T. R., Gallinari, P., Jiricny, J. and Swann, P. F. (1999) Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1. J. Biol. Chem. 274, 67-74 (Pubitemid 29035031)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 67-74
    • Waters, T.R.1    Gallinari, P.2    Jiricnyl, J.3    Swann, P.F.4
  • 39
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis, M. C. and Sinclair, D. A. (2010) Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253-295
    • (2010) Annu. Rev. Pathol , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 41
    • 33645221885 scopus 로고    scopus 로고
    • Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage
    • Solomon, J. M., Pasupuleti, R., Xu, L., McDonagh, T., Curtis, R., Di Stefano, P. S. and Huber, L. J. (2006) Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage. Mol. Cell Biol. 26, 28-38
    • (2006) Mol. Cell Biol , vol.26 , pp. 28-38
    • Solomon, J.M.1    Pasupuleti, R.2    Xu, L.3    McDonagh, T.4    Curtis, R.5    Di Stefano, P.S.6    Huber, L.J.7
  • 42
    • 77955501963 scopus 로고    scopus 로고
    • SIRT1 regulates UV-induced DNA repair through deacetylating XPA
    • Fan, W. and Luo, J. (2010) SIRT1 regulates UV-induced DNA repair through deacetylating XPA. Mol. Cell 39, 247-258
    • (2010) Mol. Cell , vol.39 , pp. 247-258
    • Fan, W.1    Luo, J.2
  • 43
    • 78649633708 scopus 로고    scopus 로고
    • Dysregulation of microRNA-34a expression causes drug-resistance to 5-FU in human colon cancer DLD-1 cells
    • Akao, Y., Noguchi, S., Iio, A., Kojima, K., Takagi, T. and Naoe, T. (2011) Dysregulation of microRNA-34a expression causes drug-resistance to 5-FU in human colon cancer DLD-1 cells. Cancer Lett. 300, 197-204
    • (2011) Cancer Lett , vol.300 , pp. 197-204
    • Akao, Y.1    Noguchi, S.2    Iio, A.3    Kojima, K.4    Takagi, T.5    Naoe, T.6
  • 45
    • 0038387494 scopus 로고    scopus 로고
    • 5-Fluorouracil: Mechanisms of action and clinical strategies
    • DOI 10.1038/nrc1074
    • Longley, D. B., Harkin, D. P. and Johnston, P. G. (2003) 5-Fluorouracil: mechanisms of action and clinical strategies. Nat. Rev. Cancer 3, 330-338 (Pubitemid 37328853)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.5 , pp. 330-338
    • Longley, D.B.1    Harkin, D.P.2    Johnston, P.G.3
  • 46
    • 65949089155 scopus 로고    scopus 로고
    • Base excision by thymine DNA glycosylase mediates DNA-directed cytotoxicity of 5-fluorouracil
    • Kunz, C., Focke, F., Saito, Y., Schuermann, D., Lettieri, T., Selfridge, J. and Schar, P. (2009) Base excision by thymine DNA glycosylase mediates DNA-directed cytotoxicity of 5-fluorouracil. PLoS Biol. 7, e91
    • (2009) PLoS Biol , vol.7
    • Kunz, C.1    Focke, F.2    Saito, Y.3    Schuermann, D.4    Lettieri, T.5    Selfridge, J.6    Schar, P.7
  • 47
    • 77649104794 scopus 로고    scopus 로고
    • Reprogramming towards pluripotency requires AID-dependent DNA demethylation
    • Bhutani, N., Brady, J. J., Damian, M., Sacco, A., Corbel, S. Y. and Blau, H. M. (2010) Reprogramming towards pluripotency requires AID-dependent DNA demethylation. Nature 463, 1042-1047
    • (2010) Nature , vol.463 , pp. 1042-1047
    • Bhutani, N.1    Brady, J.J.2    Damian, M.3    Sacco, A.4    Corbel, S.Y.5    Blau, H.M.6
  • 50
    • 10644282845 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: Implications for epigenetic reprogramming
    • DOI 10.1074/jbc.M407695200
    • Morgan, H. D., Dean, W., Coker, H. A., Reik, W. and Petersen-Mahrt, S. K. (2004) Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming. J. Biol. Chem. 279, 52353-52360 (Pubitemid 39656611)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52353-52360
    • Morgan, H.D.1    Dean, W.2    Coker, H.A.3    Reik, W.4    Petersen-Mahrt, S.K.5
  • 51
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • DOI 10.1016/j.cell.2007.01.029, PII S0092867407001274
    • Jones, P. A. and Baylin, S. B. (2007) The epigenomics of cancer. Cell 128, 683-692 (Pubitemid 46273572)
    • (2007) Cell , vol.128 , Issue.4 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2


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