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Volumn 42, Issue 10, 2014, Pages 6393-6404

Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; LYSINE; NUCLEASE; PROTEIN RAD1; RAD10 PROTEIN; SUMO PROTEIN; UNCLASSIFIED DRUG;

EID: 84903128501     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku300     Document Type: Article
Times cited : (25)

References (81)
  • 1
    • 50649091874 scopus 로고    scopus 로고
    • Structural and functional relationships of the XPF/MUS81 family of proteins
    • Ciccia, A., McDonald, N. and West, S.C. (2008) Structural and functional relationships of the XPF/MUS81 family of proteins. Annu. Rev. Biochem., 77, 259-287.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 259-287
    • Ciccia, A.1    McDonald, N.2    West, S.C.3
  • 2
    • 79955522790 scopus 로고    scopus 로고
    • Processing of joint molecule intermediates by structure-selective endonucleases during homologous recombination in eukaryotes
    • Schwartz, E.K. and Heyer, W.D. (2011) Processing of joint molecule intermediates by structure-selective endonucleases during homologous recombination in eukaryotes. Chromosoma, 120, 109-127.
    • (2011) Chromosoma , vol.120 , pp. 109-127
    • Schwartz, E.K.1    Heyer, W.D.2
  • 3
    • 67649636091 scopus 로고    scopus 로고
    • Control of genome stability by SLX protein complexes
    • Rouse, J. (2009) Control of genome stability by SLX protein complexes. Biochem. Soc. Trans., 37, 495-510.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 495-510
    • Rouse, J.1
  • 4
    • 79951573439 scopus 로고    scopus 로고
    • Functional regulation of FEN1 nuclease and its link to cancer
    • Zheng, L., Jia, J., Finger, L.D., Guo, Z., Zer, C. and Shen, B. (2011) Functional regulation of FEN1 nuclease and its link to cancer. Nucleic Acids Res., 39, 781-794.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 781-794
    • Zheng, L.1    Jia, J.2    Finger, L.D.3    Guo, Z.4    Zer, C.5    Shen, B.6
  • 5
    • 77951219621 scopus 로고    scopus 로고
    • A proteome-wide analysis of kinase-substrate network in the DNA damage response
    • Chen, S.H., Albuquerque, C.P., Liang, J., Suhandynata, R.T. and Zhou, H. (2010) A proteome-wide analysis of kinase-substrate network in the DNA damage response. J. Biol. Chem., 285, 12803-12812.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12803-12812
    • Chen, S.H.1    Albuquerque, C.P.2    Liang, J.3    Suhandynata, R.T.4    Zhou, H.5
  • 7
    • 84862783021 scopus 로고    scopus 로고
    • Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the Mec1 checkpoint
    • Cremona, C.A., Sarangi, P., Yang, Y., Hang, L.E., Rahman, S. and Zhao, X. (2012) Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the Mec1 checkpoint. Mol. Cell, 45, 422-432.
    • (2012) Mol. Cell , vol.45 , pp. 422-432
    • Cremona, C.A.1    Sarangi, P.2    Yang, Y.3    Hang, L.E.4    Rahman, S.5    Zhao, X.6
  • 8
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • Psakhye, I. and Jentsch, S. (2012) Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell, 151, 807-820.
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 11
    • 84864950070 scopus 로고    scopus 로고
    • Sequential posttranslational modifications program FEN1 degradation during cell-cycle progression
    • Guo, Z., Kanjanapangka, J., Liu, N., Liu, S., Liu, C., Wu, Z., Wang, Y., Loh, T., Kowolik, C., Jamsen, J. et al. (2012) Sequential posttranslational modifications program FEN1 degradation during cell-cycle progression. Mol. Cell, 47, 444-456.
    • (2012) Mol. Cell , vol.47 , pp. 444-456
    • Guo, Z.1    Kanjanapangka, J.2    Liu, N.3    Liu, S.4    Liu, C.5    Wu, Z.6    Wang, Y.7    Loh, T.8    Kowolik, C.9    Jamsen, J.10
  • 12
    • 80052492286 scopus 로고    scopus 로고
    • Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation
    • Chen, X., Niu, H., Chung, W.H., Zhu, Z., Papusha, A., Shim, E.Y., Lee, S.E., Sung, P. and Ira, G. (2011) Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation. Nat. Struct. Mol. Biol., 18, 1015-1019.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1015-1019
    • Chen, X.1    Niu, H.2    Chung, W.H.3    Zhu, Z.4    Papusha, A.5    Shim, E.Y.6    Lee, S.E.7    Sung, P.8    Ira, G.9
  • 14
    • 80053544629 scopus 로고    scopus 로고
    • Regulatory control of the resolution of DNA recombination intermediates during meiosis and mitosis
    • Matos, J., Blanco, M.G., Maslen, S., Skehel, J.M. and West, S.C. (2011) Regulatory control of the resolution of DNA recombination intermediates during meiosis and mitosis. Cell, 147, 158-172.
    • (2011) Cell , vol.147 , pp. 158-172
    • Matos, J.1    Blanco, M.G.2    Maslen, S.3    Skehel, J.M.4    West, S.C.5
  • 15
    • 84876407519 scopus 로고    scopus 로고
    • Premature Cdk1/Cdc5/Mus81 pathway activation induces aberrant replication and deleterious crossover
    • Szakal, B. and Branzei, D. (2013) Premature Cdk1/Cdc5/Mus81 pathway activation induces aberrant replication and deleterious crossover. EMBO J., 32, 1155-1167.
    • (2013) EMBO J. , vol.32 , pp. 1155-1167
    • Szakal, B.1    Branzei, D.2
  • 17
    • 2942594756 scopus 로고    scopus 로고
    • The functions of budding yeast Sae2 in the DNA damage response require Mec1- and Tel1-dependent phosphorylation
    • Baroni, E., Viscardi, V., Cartagena-Lirola, H., Lucchini, G. and Longhese, M.P. (2004) The functions of budding yeast Sae2 in the DNA damage response require Mec1- and Tel1-dependent phosphorylation. Mol. Cell Biol., 24, 4151-4165.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 4151-4165
    • Baroni, E.1    Viscardi, V.2    Cartagena-Lirola, H.3    Lucchini, G.4    Longhese, M.P.5
  • 18
    • 53349162987 scopus 로고    scopus 로고
    • CDK targets Sae2 to control DNA-end resection and homologous recombination
    • Huertas, P., Cortes-Ledesma, F., Sartori, A.A., Aguilera, A. and Jackson, S.P. (2008) CDK targets Sae2 to control DNA-end resection and homologous recombination. Nature, 455, 689-692.
    • (2008) Nature , vol.455 , pp. 689-692
    • Huertas, P.1    Cortes-Ledesma, F.2    Sartori, A.A.3    Aguilera, A.4    Jackson, S.P.5
  • 19
    • 0035449349 scopus 로고    scopus 로고
    • The yeast Xrs2 complex functions in S phase checkpoint regulation
    • D'Amours, D. and Jackson, S.P. (2001) The yeast Xrs2 complex functions in S phase checkpoint regulation. Genes Dev., 15, 2238-2249.
    • (2001) Genes Dev. , vol.15 , pp. 2238-2249
    • D'Amours, D.1    Jackson, S.P.2
  • 22
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao, X. and Blobel, G. (2005) A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl. Acad. Sci. U.S.A., 102, 4777-4782.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.2
  • 23
    • 72449175818 scopus 로고    scopus 로고
    • Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks
    • Galanty, Y., Belotserkovskaya, R., Coates, J., Polo, S., Miller, K.M. and Jackson, S.P. (2009) Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks. Nature, 462, 935-939.
    • (2009) Nature , vol.462 , pp. 935-939
    • Galanty, Y.1    Belotserkovskaya, R.2    Coates, J.3    Polo, S.4    Miller, K.M.5    Jackson, S.P.6
  • 24
    • 33750437743 scopus 로고    scopus 로고
    • Ubc9- and Mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks
    • Branzei, D., Sollier, J., Liberi, G., Zhao, X., Maeda, D., Seki, M., Enomoto, T., Ohta, K. and Foiani, M. (2006) Ubc9- and Mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks. Cell, 127, 509-522.
    • (2006) Cell , vol.127 , pp. 509-522
    • Branzei, D.1    Sollier, J.2    Liberi, G.3    Zhao, X.4    Maeda, D.5    Seki, M.6    Enomoto, T.7    Ohta, K.8    Foiani, M.9
  • 25
    • 0842281642 scopus 로고    scopus 로고
    • Ubc9 is required for damage-tolerance and damage-induced interchromosomal homologous recombination in S cerevisiae
    • Maeda, D., Seki, M., Onoda, F., Branzei, D., Kawabe, Y. and Enomoto, T. (2004) Ubc9 is required for damage-tolerance and damage-induced interchromosomal homologous recombination in S. cerevisiae. DNA Repair 3, 335-341.
    • (2004) DNA Repair , vol.3 , pp. 335-341
    • Maeda, D.1    Seki, M.2    Onoda, F.3    Branzei, D.4    Kawabe, Y.5    Enomoto, T.6
  • 26
    • 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. and Friedberg, E.C. (1994) Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease. Science, 265, 2082-2085.
    • (1994) Science , vol.265 , pp. 2082-2085
    • Bardwell, A.J.1    Bardwell, L.2    Tomkinson, A.E.3    Friedberg, E.C.4
  • 27
    • 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. and West, S.C. (1995) Role of the Rad1 and Rad10 proteins in nucleotide excision repair and recombination. J. Biol. Chem., 270, 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
  • 28
    • 0027365033 scopus 로고
    • Purification and characterization of the Saccharomyces cerevisiae Rad1/Rad10 endonuclease
    • Sung, P., Reynolds, P., Prakash, L. and Prakash, S. (1993) Purification and characterization of the Saccharomyces cerevisiae Rad1/Rad10 endonuclease. J. Biol. Chem., 268, 26391-26399.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26391-26399
    • Sung, P.1    Reynolds, P.2    Prakash, L.3    Prakash, S.4
  • 30
    • 77958535871 scopus 로고    scopus 로고
    • Multiple roles of the ERCC1-XPF endonuclease in DNA repair and resistance to anticancer drugs
    • Kirschner, K. and Melton, D.W. (2010) Multiple roles of the ERCC1-XPF endonuclease in DNA repair and resistance to anticancer drugs. Anticancer Res., 30, 3223-3232.
    • (2010) Anticancer Res. , vol.30 , pp. 3223-3232
    • Kirschner, K.1    Melton, D.W.2
  • 31
    • 79960394750 scopus 로고    scopus 로고
    • Physiological consequences of defects in ERCC1-XPF DNA repair endonuclease
    • Gregg, S.Q., Robinson, A.R. and Niedernhofer, L.J. (2011) Physiological consequences of defects in ERCC1-XPF DNA repair endonuclease. DNA Repair 10, 781-791.
    • (2011) DNA Repair , vol.10 , pp. 781-791
    • Gregg, S.Q.1    Robinson, A.R.2    Niedernhofer, L.J.3
  • 33
    • 0033988552 scopus 로고    scopus 로고
    • Damage recognition in nucleotide excision repair of DNA
    • Batty, D.P. and Wood, R.D. (2000) Damage recognition in nucleotide excision repair of DNA. Gene, 241, 193-204.
    • (2000) Gene , vol.241 , pp. 193-204
    • Batty, D.P.1    Wood, R.D.2
  • 34
    • 0032553414 scopus 로고    scopus 로고
    • Affinity of yeast nucleotide excision repair factor 2, consisting of the Rad4 and Rad23 proteins, for ultraviolet damaged DNA
    • Guzder, S.N., Sung, P., Prakash, L. and Prakash, S. (1998) Affinity of yeast nucleotide excision repair factor 2, consisting of the Rad4 and Rad23 proteins, for ultraviolet damaged DNA. J. Biol. Chem., 273, 31541-31546.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31541-31546
    • Guzder, S.N.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 35
    • 0032509333 scopus 로고    scopus 로고
    • Preferential binding of yeast Rad4. Rad23 complex to damaged DNA
    • Jansen, L.E., Verhage, R.A. and Brouwer, J. (1998) Preferential binding of yeast Rad4. Rad23 complex to damaged DNA. J. Biol. Chem., 273, 33111-33114.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33111-33114
    • Jansen, L.E.1    Verhage, R.A.2    Brouwer, J.3
  • 36
    • 15844390308 scopus 로고    scopus 로고
    • Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair
    • Sung, P., Guzder, S.N., Prakash, L. and Prakash, S. (1996) Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair. J. Biol. Chem., 271, 10821-10826.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10821-10826
    • Sung, P.1    Guzder, S.N.2    Prakash, L.3    Prakash, S.4
  • 37
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans, E., Moggs, J.G., Hwang, J.R., Egly, J.M. and Wood, R.D. (1997) Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J., 16, 6559-6573.
    • (1997) EMBO J. , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.M.4    Wood, R.D.5
  • 38
    • 31344443061 scopus 로고    scopus 로고
    • Complex formation with damage recognition protein Rad14 is essential for Saccharomyces cerevisiae Rad1-Rad10 nuclease to perform its function in nucleotide excision repair in vivo
    • Guzder, S.N., Sommers, C.H., Prakash, L. and Prakash, S. (2006) Complex formation with damage recognition protein Rad14 is essential for Saccharomyces cerevisiae Rad1-Rad10 nuclease to perform its function in nucleotide excision repair in vivo. Mol. Cell Biol., 26, 1135-1141.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 1135-1141
    • Guzder, S.N.1    Sommers, C.H.2    Prakash, L.3    Prakash, S.4
  • 40
    • 0029019788 scopus 로고
    • Reconstitution of yeast nucleotide excision repair with purified Rad proteins, replication protein A, and transcription factor TFIIH
    • Guzder, S.N., Habraken, Y., Sung, P., Prakash, L. and Prakash, S. (1995) Reconstitution of yeast nucleotide excision repair with purified Rad proteins, replication protein A, and transcription factor TFIIH. J. Biol. Chem., 270, 12973-12976.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12973-12976
    • Guzder, S.N.1    Habraken, Y.2    Sung, P.3    Prakash, L.4    Prakash, S.5
  • 41
    • 0029784467 scopus 로고    scopus 로고
    • Transcription factor TFIIH and DNA endonuclease Rad2 constitute yeast nucleotide excision repair factor 3: Implications for nucleotide excision repair and Cockayne syndrome
    • Habraken, Y., Sung, P., Prakash, S. and Prakash, L. (1996) Transcription factor TFIIH and DNA endonuclease Rad2 constitute yeast nucleotide excision repair factor 3: implications for nucleotide excision repair and Cockayne syndrome. Proc. Natl. Acad. Sci. U.S.A., 93, 10718-10722.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10718-10722
    • Habraken, Y.1    Sung, P.2    Prakash, S.3    Prakash, L.4
  • 42
    • 0037108948 scopus 로고    scopus 로고
    • Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage
    • Vance, J.R. and Wilson, T.E. (2002) Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage. Proc. Natl. Acad. Sci. U.S.A., 99, 13669-13674.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13669-13674
    • Vance, J.R.1    Wilson, T.E.2
  • 43
    • 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. and Boiteux, S. (2002) Endogenous DNA abasic sites cause cell death in the absence of Apn1, Apn2 and Rad1/Rad10 in Saccharomyces cerevisiae. EMBO J., 21, 2833-2841.
    • (2002) EMBO J. , vol.21 , pp. 2833-2841
    • Guillet, M.1    Boiteux, S.2
  • 44
    • 10344263324 scopus 로고    scopus 로고
    • Recombination proteins in yeast
    • Krogh, B.O. and Symington, L.S. (2004) Recombination proteins in yeast. Annu. Rev. Genet., 38, 233-271.
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 233-271
    • Krogh, B.O.1    Symington, L.S.2
  • 45
    • 50649100744 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo, J., Sung, P. and Klein, H. (2008) Mechanism of eukaryotic homologous recombination. Annu. Rev. Biochem., 77, 229-257.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 229-257
    • San Filippo, J.1    Sung, P.2    Klein, H.3
  • 46
    • 43049111100 scopus 로고    scopus 로고
    • Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediates
    • Li, F., Dong, J., Pan, X., Oum, J.H., Boeke, J.D. and Lee, S.E. (2008) Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediates. Mol. Cell, 30, 325-335.
    • (2008) Mol. Cell , vol.30 , pp. 325-335
    • Li, F.1    Dong, J.2    Pan, X.3    Oum, J.H.4    Boeke, J.D.5    Lee, S.E.6
  • 48
    • 77952581455 scopus 로고    scopus 로고
    • Mec1/Tel1-dependent phosphorylation of Slx4 stimulates Rad1-Rad10-dependent cleavage of non-homologous DNA tails
    • Toh, G.W., Sugawara, N., Dong, J., Toth, R., Lee, S.E., Haber, J.E. and Rouse, J. (2010) Mec1/Tel1-dependent phosphorylation of Slx4 stimulates Rad1-Rad10-dependent cleavage of non-homologous DNA tails. DNA Repair 9, 718-726.
    • (2010) DNA Repair , vol.9 , pp. 718-726
    • Toh, G.W.1    Sugawara, N.2    Dong, J.3    Toth, R.4    Lee, S.E.5    Haber, J.E.6    Rouse, J.7
  • 49
    • 34548213631 scopus 로고    scopus 로고
    • The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination
    • Burgess, R.C., Rahman, S., Lisby, M., Rothstein, R. and Zhao, X. (2007) The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination. Mol. Cell Biol., 27, 6153-6162.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 6153-6162
    • Burgess, R.C.1    Rahman, S.2    Lisby, M.3    Rothstein, R.4    Zhao, X.5
  • 50
    • 0032581214 scopus 로고    scopus 로고
    • Curing Saccharomyces cerevisiae of the 2 micron plasmid by targeted DNA damage
    • Tsalik, E.L. and Gartenberg, M.R. (1998) Curing Saccharomyces cerevisiae of the 2 micron plasmid by targeted DNA damage. Yeast, 14, 847-852.
    • (1998) Yeast , vol.14 , pp. 847-852
    • Tsalik, E.L.1    Gartenberg, M.R.2
  • 51
    • 79961029209 scopus 로고    scopus 로고
    • SUMOylation regulates telomere length homeostasis by targeting Cdc13
    • Hang, L.E., Liu, X., Cheung, I., Yang, Y. and Zhao, X. (2011) SUMOylation regulates telomere length homeostasis by targeting Cdc13. Nat. Struct. Mol. Biol., 18, 920-926.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 920-926
    • Hang, L.E.1    Liu, X.2    Cheung, I.3    Yang, Y.4    Zhao, X.5
  • 52
    • 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. and Brill, S.J. (2003) The mechanism of Mus81-Mms4 cleavage site selection distinguishes it from the homologous endonuclease Rad1-Rad10. Mol. Cell Biol., 23, 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
  • 54
    • 65549118806 scopus 로고    scopus 로고
    • Cooperativity of Mus81. Mms4 with Rad54 in the resolution of recombination and replication intermediates
    • Matulova, P., Marini, V., Burgess, R.C., Sisakova, A., Kwon, Y., Rothstein, R., Sung, P. and Krejci, L. (2009) Cooperativity of Mus81. Mms4 with Rad54 in the resolution of recombination and replication intermediates. J. Biol. Chem., 284, 7733-7745.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7733-7745
    • Matulova, P.1    Marini, V.2    Burgess, R.C.3    Sisakova, A.4    Kwon, Y.5    Rothstein, R.6    Sung, P.7    Krejci, L.8
  • 55
    • 0034733496 scopus 로고    scopus 로고
    • Nucleotide excision repair in yeast
    • Prakash, S. and Prakash, L. (2000) Nucleotide excision repair in yeast. Mutat. Res., 451, 13-24.
    • (2000) Mutat. Res. , vol.451 , pp. 13-24
    • Prakash, S.1    Prakash, L.2
  • 56
    • 65249160271 scopus 로고    scopus 로고
    • A tale of tails: Insights into the coordination of 3' end processing during homologous recombination
    • Lyndaker, A.M. and Alani, E. (2009) A tale of tails: insights into the coordination of 3' end processing during homologous recombination. Bioessays, 31, 315-321.
    • (2009) Bioessays , vol.31 , pp. 315-321
    • Lyndaker, A.M.1    Alani, E.2
  • 57
    • 0037090816 scopus 로고    scopus 로고
    • The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif
    • Enzlin, J.H. and Scharer, O.D. (2002) The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif. EMBO J., 21, 2045-2053.
    • (2002) EMBO J. , vol.21 , pp. 2045-2053
    • Enzlin, J.H.1    Scharer, O.D.2
  • 58
  • 59
    • 34548747505 scopus 로고    scopus 로고
    • Phosphorylation of Slx4 by Mec1 and Tel1 regulates the single-strand annealing mode of DNA repair in budding yeast
    • Flott, S., Alabert, C., Toh, G.W., Toth, R., Sugawara, N., Campbell, D.G., Haber, J.E., Pasero, P. and Rouse, J. (2007) Phosphorylation of Slx4 by Mec1 and Tel1 regulates the single-strand annealing mode of DNA repair in budding yeast. Mol. Cell Biol., 27, 6433-6445.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 6433-6445
    • Flott, S.1    Alabert, C.2    Toh, G.W.3    Toth, R.4    Sugawara, N.5    Campbell, D.G.6    Haber, J.E.7    Pasero, P.8    Rouse, J.9
  • 60
    • 85016362060 scopus 로고    scopus 로고
    • Sumoylation and the DNA damage response
    • Cremona, C.A., Sarangi, P. and Zhao, X. (2012) Sumoylation and the DNA Damage Response. Biomolecules, 2, 376-388.
    • (2012) Biomolecules , vol.2 , pp. 376-388
    • Cremona, C.A.1    Sarangi, P.2    Zhao, X.3
  • 61
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E.S. (2004) Protein modification by SUMO. Annu. Rev. Biochem., 73, 355-382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 62
    • 59149107480 scopus 로고    scopus 로고
    • The SUMO system: An overview
    • Ulrich, H.D. (2009) The SUMO system: an overview. Methods Mol. Biol., 497, 3-16.
    • (2009) Methods Mol. Biol. , vol.497 , pp. 3-16
    • Ulrich, H.D.1
  • 63
    • 74949127215 scopus 로고    scopus 로고
    • Detection of proteins sumoylated in vivo and in vitro
    • Sarge, K.D. and Park-Sarge, O.K. (2009) Detection of proteins sumoylated in vivo and in vitro. Methods Mol. Biol., 590, 265-277.
    • (2009) Methods Mol. Biol. , vol.590 , pp. 265-277
    • Sarge, K.D.1    Park-Sarge, O.K.2
  • 64
    • 38049079191 scopus 로고    scopus 로고
    • Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae
    • Windecker, H. and Ulrich, H.D. (2008) Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae. J. Mol. Biol., 376, 221-231.
    • (2008) J. Mol. Biol. , vol.376 , pp. 221-231
    • Windecker, H.1    Ulrich, H.D.2
  • 65
    • 0037907672 scopus 로고    scopus 로고
    • Comparative analysis of yeast PIAS-type SUMO ligases in vivo and in vitro
    • Takahashi, Y., Toh, E.A. and Kikuchi, Y. (2003) Comparative analysis of yeast PIAS-type SUMO ligases in vivo and in vitro. J. Biochem., 133, 415-422.
    • (2003) J. Biochem. , vol.133 , pp. 415-422
    • Takahashi, Y.1    Toh, E.A.2    Kikuchi, Y.3
  • 66
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M.S., Dargemont, C. and Hay, R.T. (2001) SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem., 276, 12654-12659.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 67
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson, D.A., Wang, M. and Matunis, M.J. (2001) The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem., 276, 21664-21669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 68
    • 84864448524 scopus 로고    scopus 로고
    • Fluorescence-based incision assay for human XPF-ERCC1 activity identifies important elements of DNA junction recognition
    • Bowles, M., Lally, J., Fadden, A.J., Mouilleron, S., Hammonds, T. and McDonald, N.Q. (2012) Fluorescence-based incision assay for human XPF-ERCC1 activity identifies important elements of DNA junction recognition. Nucleic Acids Res., 40, e101.
    • (2012) Nucleic Acids Res. , vol.40
    • Bowles, M.1    Lally, J.2    Fadden, A.J.3    Mouilleron, S.4    Hammonds, T.5    McDonald, N.Q.6
  • 69
    • 33745154128 scopus 로고    scopus 로고
    • Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage
    • Nitiss, K.C., Malik, M., He, X., White, S.W. and Nitiss, J.L. (2006) Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage. Proc. Natl. Acad. Sci. U. S. A., 103, 8953-8958.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8953-8958
    • Nitiss, K.C.1    Malik, M.2    He, X.3    White, S.W.4    Nitiss, J.L.5
  • 70
    • 0348140585 scopus 로고    scopus 로고
    • Abasic sites in DNA: Repair and biological consequences in Saccharomyces cerevisiae
    • Boiteux, S. and Guillet, M. (2004) Abasic sites in DNA: repair and biological consequences in Saccharomyces cerevisiae. DNA Repair 3, 1-12.
    • (2004) DNA Repair , vol.3 , pp. 1-12
    • Boiteux, S.1    Guillet, M.2
  • 71
    • 4444281763 scopus 로고    scopus 로고
    • Requirement of yeast Rad1-Rad10 nuclease for the removal of 3'-blocked termini from DNA strand breaks induced by reactive oxygen species
    • Guzder, S.N., Torres-Ramos, C., Johnson, R.E., Haracska, L., Prakash, L. and Prakash, S. (2004) Requirement of yeast Rad1-Rad10 nuclease for the removal of 3'-blocked termini from DNA strand breaks induced by reactive oxygen species. Genes Dev., 18, 2283-2291.
    • (2004) Genes Dev. , vol.18 , pp. 2283-2291
    • Guzder, S.N.1    Torres-Ramos, C.2    Johnson, R.E.3    Haracska, L.4    Prakash, L.5    Prakash, S.6
  • 72
    • 27444444448 scopus 로고    scopus 로고
    • Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent manner and is required for repair of DNA alkylation damage
    • Flott, S. and Rouse, J. (2005) Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent manner and is required for repair of DNA alkylation damage. Biochem J., 391, 325-333.
    • (2005) Biochem J. , vol.391 , pp. 325-333
    • Flott, S.1    Rouse, J.2
  • 73
    • 84880562168 scopus 로고    scopus 로고
    • Nucleotide excision repair in human cells: Fate of the excised oligonucleotide carrying DNA damage in vivo
    • Hu, J., Choi, J.H., Gaddameedhi, S., Kemp, M.G., Reardon, J.T. and Sancar, A. (2013) Nucleotide excision repair in human cells: fate of the excised oligonucleotide carrying DNA damage in vivo. J. Biol. Chem., 288, 20918-20926.
    • (2013) J. Biol. Chem. , vol.288 , pp. 20918-20926
    • Hu, J.1    Choi, J.H.2    Gaddameedhi, S.3    Kemp, M.G.4    Reardon, J.T.5    Sancar, A.6
  • 74
    • 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
  • 75
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland, U., Steinacher, R., Jiricny, J. and Schar, P. (2002) Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J., 21, 1456-1464.
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 77
    • 67649182975 scopus 로고    scopus 로고
    • Rpb1 sumoylation in response to UV radiation or transcriptional impairment in yeast
    • Chen, X., Ding, B., LeJeune, D., Ruggiero, C. and Li, S. (2009) Rpb1 sumoylation in response to UV radiation or transcriptional impairment in yeast. PLoS One, 4, e5267.
    • (2009) PLoS One , vol.4
    • Chen, X.1    Ding, B.2    Lejeune, D.3    Ruggiero, C.4    Li, S.5
  • 78
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G.L., Pyrowolakis, G. and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature, 419, 135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 79
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli, E., Chen, S., Davies, A.A., Huttner, D., Krejci, L., Sung, P. and Ulrich, H.D. (2005) Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol. Cell, 19, 123-133.
    • (2005) Mol. Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 80
    • 84898619525 scopus 로고    scopus 로고
    • Regulation of Ku-DNA association by Yku70 C-terminal tail and SUMO modification
    • doi:10.1074/jbc.M113.526178; epub ahead of print February 24, 2014
    • Hang, L.E., Lopez, C.R., Liu, X., Williams, J.M., Chung, I., Wei, L., Bertuch, A.A. and Zhao, X. (2014) Regulation of Ku-DNA association by Yku70 C-terminal tail and SUMO modification. J. Biol. Chem., doi:10.1074/jbc.M113. 526178; epub ahead of print February 24, 2014.
    • (2014) J. Biol. Chem.
    • Hang, L.E.1    Lopez, C.R.2    Liu, X.3    Williams, J.M.4    Chung, I.5    Wei, L.6    Bertuch, A.A.7    Zhao, X.8
  • 81
    • 33750499289 scopus 로고    scopus 로고
    • Control of Rad52 recombination activity by double-strand break-induced SUMO modification
    • Sacher, M., Pfander, B., Hoege, C. and Jentsch, S. (2006) Control of Rad52 recombination activity by double-strand break-induced SUMO modification. Nat. Cell Biol., 8, 1284-1290.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1284-1290
    • Sacher, M.1    Pfander, B.2    Hoege, C.3    Jentsch, S.4


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