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Volumn 8, Issue 9, 2009, Pages 974-982

Perspectives on the DNA damage and replication checkpoint responses in Saccharomyces cerevisiae

Author keywords

Cell cycle checkpoint; DNA damage; DNA repair; Genome stability; Positive feedback; Transcriptional response

Indexed keywords

ATM PROTEIN; ATR PROTEIN; CHECKPOINT KINASE 1; CHECKPOINT KINASE 2; DNA; MEC 1 PROTEIN; PROTEIN TEL 1; SACCHAROMYCES CEREVISIAE PROTEIN; UNCLASSIFIED DRUG;

EID: 68249099217     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2009.04.021     Document Type: Article
Times cited : (65)

References (137)
  • 1
    • 0023712476 scopus 로고
    • The RAD9 gene controls the cell cycle response to DNA damage in Saccharomyces cerevisiae
    • Weinert T.A., and 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
  • 2
    • 0027338038 scopus 로고
    • RAD9-dependent G1 arrest defines a second checkpoint for damaged DNA in the cell cycle of Saccharomyces cerevisiae
    • Siede W., Friedberg A.S., and Friedberg E.C. RAD9-dependent G1 arrest defines a second checkpoint for damaged DNA in the cell cycle of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 7985-7989
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7985-7989
    • Siede, W.1    Friedberg, A.S.2    Friedberg, E.C.3
  • 3
    • 0032497529 scopus 로고    scopus 로고
    • A Mec1- and Rad53-dependent checkpoint controls late-firing origins of DNA replication
    • Santocanale C., and Diffley J.F. A Mec1- and Rad53-dependent checkpoint controls late-firing origins of DNA replication. Nature 395 (1998) 615-618
    • (1998) Nature , vol.395 , pp. 615-618
    • Santocanale, C.1    Diffley, J.F.2
  • 4
    • 0031036995 scopus 로고    scopus 로고
    • RAD9, RAD17, and RAD24 are required for S phase regulation in Saccharomyces cerevisiae in response to DNA damage
    • Paulovich A.G., Margulies R.U., Garvik B.M., and Hartwell L.H. RAD9, RAD17, and RAD24 are required for S phase regulation in Saccharomyces cerevisiae in response to DNA damage. Genetics 145 (1997) 45-62
    • (1997) Genetics , vol.145 , pp. 45-62
    • Paulovich, A.G.1    Margulies, R.U.2    Garvik, B.M.3    Hartwell, L.H.4
  • 5
    • 0037007074 scopus 로고    scopus 로고
    • Suppression of genome instability by redundant S-phase checkpoint pathways in Saccharomyces cerevisiae
    • Myung K., and Kolodner R.D. Suppression of genome instability by redundant S-phase checkpoint pathways in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 4500-4507
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4500-4507
    • Myung, K.1    Kolodner, R.D.2
  • 6
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
    • Zou L., and Elledge S.J. Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science 300 (2003) 1542-1548
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2
  • 7
    • 0041660970 scopus 로고    scopus 로고
    • ATM-related Tel1 associates with double-strand breaks through an Xrs2-dependent mechanism
    • Nakada D., Matsumoto K., and Sugimoto K. ATM-related Tel1 associates with double-strand breaks through an Xrs2-dependent mechanism. Genes Dev. 17 (2003) 1957-1962
    • (2003) Genes Dev. , vol.17 , pp. 1957-1962
    • Nakada, D.1    Matsumoto, K.2    Sugimoto, K.3
  • 8
    • 0032793298 scopus 로고    scopus 로고
    • Interactions of TLC1 (which encodes the RNA subunit of telomerase), TEL1, and MEC1 in regulating telomere length in the yeast Saccharomyces cerevisiae
    • Ritchie K.B., Mallory J.C., and Petes T.D. Interactions of TLC1 (which encodes the RNA subunit of telomerase), TEL1, and MEC1 in regulating telomere length in the yeast Saccharomyces cerevisiae. Mol. Cell Biol. 19 (1999) 6065-6075
    • (1999) Mol. Cell Biol. , vol.19 , pp. 6065-6075
    • Ritchie, K.B.1    Mallory, J.C.2    Petes, T.D.3
  • 9
    • 0035928740 scopus 로고    scopus 로고
    • Altering telomere structure allows telomerase to act in yeast lacking ATM kinases
    • Chan S.W., Chang J., Prescott J., and Blackburn E.H. Altering telomere structure allows telomerase to act in yeast lacking ATM kinases. Curr. Biol. 11 (2001) 1240-1250
    • (2001) Curr. Biol. , vol.11 , pp. 1240-1250
    • Chan, S.W.1    Chang, J.2    Prescott, J.3    Blackburn, E.H.4
  • 10
    • 0029150855 scopus 로고
    • TEL1, an S. cerevisiae homolog of the human gene mutated in ataxia telangiectasia, is functionally related to the yeast checkpoint gene MEC1
    • Morrow D.M., Tagle D.A., Shiloh Y., Collins F.S., and Hieter P. TEL1, an S. cerevisiae homolog of the human gene mutated in ataxia telangiectasia, is functionally related to the yeast checkpoint gene MEC1. Cell 82 (1995) 831-840
    • (1995) Cell , vol.82 , pp. 831-840
    • Morrow, D.M.1    Tagle, D.A.2    Shiloh, Y.3    Collins, F.S.4    Hieter, P.5
  • 11
    • 0034700511 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae histone H2A in DNA repair
    • Downs J.A., Lowndes N.F., and Jackson S.P. A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature 408 (2000) 1001-1004
    • (2000) Nature , vol.408 , pp. 1001-1004
    • Downs, J.A.1    Lowndes, N.F.2    Jackson, S.P.3
  • 12
    • 0000393532 scopus 로고
    • Identification of yeast mutants with altered telomere structure
    • Lustig A.J., and Petes T.D. Identification of yeast mutants with altered telomere structure. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 1398-1402
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 1398-1402
    • Lustig, A.J.1    Petes, T.D.2
  • 14
    • 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. CDK targets Sae2 to control DNA-end resection and homologous recombination. Nature 455 (2008) 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
  • 15
    • 0035955398 scopus 로고    scopus 로고
    • Recruitment of Mec1 and Ddc1 checkpoint proteins to double-strand breaks through distinct mechanisms
    • Kondo T., Wakayama T., Naiki T., Matsumoto K., and Sugimoto K. Recruitment of Mec1 and Ddc1 checkpoint proteins to double-strand breaks through distinct mechanisms. Science 294 (2001) 867-870
    • (2001) Science , vol.294 , pp. 867-870
    • Kondo, T.1    Wakayama, T.2    Naiki, T.3    Matsumoto, K.4    Sugimoto, K.5
  • 16
    • 0035498938 scopus 로고    scopus 로고
    • Two checkpoint complexes are independently recruited to sites of DNA damage in vivo
    • Melo J.A., Cohen J., and Toczyski D.P. Two checkpoint complexes are independently recruited to sites of DNA damage in vivo. Genes Dev. 15 (2001) 2809-2821
    • (2001) Genes Dev. , vol.15 , pp. 2809-2821
    • Melo, J.A.1    Cohen, J.2    Toczyski, D.P.3
  • 17
    • 33845607102 scopus 로고    scopus 로고
    • The checkpoint clamp activates Mec1 kinase during initiation of the DNA damage checkpoint
    • Majka J., Niedziela-Majka A., and Burgers P.M. The checkpoint clamp activates Mec1 kinase during initiation of the DNA damage checkpoint. Mol. Cell 24 (2006) 891-901
    • (2006) Mol. Cell , vol.24 , pp. 891-901
    • Majka, J.1    Niedziela-Majka, A.2    Burgers, P.M.3
  • 18
    • 42949130159 scopus 로고    scopus 로고
    • Colocalization of sensors is sufficient to activate the DNA damage checkpoint in the absence of damage
    • Bonilla C.Y., Melo J.A., and Toczyski D.P. Colocalization of sensors is sufficient to activate the DNA damage checkpoint in the absence of damage. Mol. Cell 30 (2008) 267-276
    • (2008) Mol. Cell , vol.30 , pp. 267-276
    • Bonilla, C.Y.1    Melo, J.A.2    Toczyski, D.P.3
  • 19
    • 0242287930 scopus 로고    scopus 로고
    • Hiding at the ends of yeast chromosomes: telomeres, nucleases and checkpoint pathways
    • Lydall D. Hiding at the ends of yeast chromosomes: telomeres, nucleases and checkpoint pathways. J. Cell Sci. 116 (2003) 4057-4065
    • (2003) J. Cell Sci. , vol.116 , pp. 4057-4065
    • Lydall, D.1
  • 21
    • 58149102035 scopus 로고    scopus 로고
    • Yeast DNA replication protein Dpb11 activates the Mec1/ATR checkpoint kinase
    • Navadgi-Patil V.M., and Burgers P.M. Yeast DNA replication protein Dpb11 activates the Mec1/ATR checkpoint kinase. J. Biol. Chem. 283 (2008) 35853-35859
    • (2008) J. Biol. Chem. , vol.283 , pp. 35853-35859
    • Navadgi-Patil, V.M.1    Burgers, P.M.2
  • 22
    • 34250705797 scopus 로고    scopus 로고
    • The Rad9-Hus1-Rad1 (9-1-1) clamp activates checkpoint signaling via TopBP1
    • Delacroix S., Wagner J.M., Kobayashi M., Yamamoto K., and Karnitz L.M. The Rad9-Hus1-Rad1 (9-1-1) clamp activates checkpoint signaling via TopBP1. Genes Dev. 21 (2007) 1472-1477
    • (2007) Genes Dev. , vol.21 , pp. 1472-1477
    • Delacroix, S.1    Wagner, J.M.2    Kobayashi, M.3    Yamamoto, K.4    Karnitz, L.M.5
  • 23
    • 2442646547 scopus 로고    scopus 로고
    • Chk1 activation requires Rad9 S/TQ-site phosphorylation to promote association with C-terminal BRCT domains of Rad4TOPBP1
    • Furuya K., Poitelea M., Guo L., Caspari T., and Carr A.M. Chk1 activation requires Rad9 S/TQ-site phosphorylation to promote association with C-terminal BRCT domains of Rad4TOPBP1. Genes Dev. 18 (2004) 1154-1164
    • (2004) Genes Dev. , vol.18 , pp. 1154-1164
    • Furuya, K.1    Poitelea, M.2    Guo, L.3    Caspari, T.4    Carr, A.M.5
  • 24
    • 34948889415 scopus 로고    scopus 로고
    • The Rad9-Hus1-Rad1 checkpoint clamp regulates interaction of TopBP1 with ATR
    • Lee J., Kumagai A., and Dunphy W.G. The Rad9-Hus1-Rad1 checkpoint clamp regulates interaction of TopBP1 with ATR. J. Biol. Chem. 282 (2007) 28036-28044
    • (2007) J. Biol. Chem. , vol.282 , pp. 28036-28044
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 25
    • 0026610360 scopus 로고
    • Regulation of p34CDC28 tyrosine phosphorylation is not required for entry into mitosis in S. cerevisiae
    • Amon A., Surana U., Muroff I., and Nasmyth K. Regulation of p34CDC28 tyrosine phosphorylation is not required for entry into mitosis in S. cerevisiae. Nature 355 (1992) 368-371
    • (1992) Nature , vol.355 , pp. 368-371
    • Amon, A.1    Surana, U.2    Muroff, I.3    Nasmyth, K.4
  • 26
    • 0026567896 scopus 로고
    • S-phase feedback control in budding yeast independent of tyrosine phosphorylation of p34cdc28
    • Sorger P.K., and Murray A.W. S-phase feedback control in budding yeast independent of tyrosine phosphorylation of p34cdc28. Nature 355 (1992) 365-368
    • (1992) Nature , vol.355 , pp. 365-368
    • Sorger, P.K.1    Murray, A.W.2
  • 27
    • 0035101733 scopus 로고    scopus 로고
    • Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1
    • Emili A., Schieltz D.M., Yates J.R., and Hartwell III L.H. Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1. Mol. Cell 7 (2001) 13-20
    • (2001) Mol. Cell , vol.7 , pp. 13-20
    • Emili, A.1    Schieltz, D.M.2    Yates, J.R.3    Hartwell III, L.H.4
  • 28
    • 0035336971 scopus 로고    scopus 로고
    • Asf1 links Rad53 to control of chromatin assembly
    • Hu F., Alcasabas A.A., and Elledge S.J. Asf1 links Rad53 to control of chromatin assembly. Genes Dev. 15 (2001) 1061-1066
    • (2001) Genes Dev. , vol.15 , pp. 1061-1066
    • Hu, F.1    Alcasabas, A.A.2    Elledge, S.J.3
  • 29
    • 32544458906 scopus 로고    scopus 로고
    • Regulation of histone deposition proteins Asf1/Hir1 by multiple DNA damage checkpoint kinases in Saccharomyces cerevisiae
    • Sharp J.A., Rizki G., and Kaufman P.D. Regulation of histone deposition proteins Asf1/Hir1 by multiple DNA damage checkpoint kinases in Saccharomyces cerevisiae. Genetics 171 (2005) 885-899
    • (2005) Genetics , vol.171 , pp. 885-899
    • Sharp, J.A.1    Rizki, G.2    Kaufman, P.D.3
  • 30
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen C.C., Carson J.J., Feser J., Tamburini B., Zabaronick S., Linger J., and Tyler J.K. Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 134 (2008) 231-243
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 32
    • 0036281710 scopus 로고    scopus 로고
    • Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint
    • Schwartz M.F., Duong J.K., Sun Z., Morrow J.S., Pradhan D., and Stern D.F. Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint. Mol. Cell 9 (2002) 1055-1065
    • (2002) Mol. Cell , vol.9 , pp. 1055-1065
    • Schwartz, M.F.1    Duong, J.K.2    Sun, Z.3    Morrow, J.S.4    Pradhan, D.5    Stern, D.F.6
  • 33
    • 0038506000 scopus 로고    scopus 로고
    • Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53
    • Osborn A.J., and Elledge S.J. Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53. Genes Dev. 17 (2003) 1755-1767
    • (2003) Genes Dev. , vol.17 , pp. 1755-1767
    • Osborn, A.J.1    Elledge, S.J.2
  • 34
    • 9444260451 scopus 로고    scopus 로고
    • A Ddc2-Rad53 fusion protein can bypass the requirements for RAD9 and MRC1 in Rad53 activation
    • Lee S.J., Duong J.K., and Stern D.F. A Ddc2-Rad53 fusion protein can bypass the requirements for RAD9 and MRC1 in Rad53 activation. Mol. Biol. Cell 15 (2004) 5443-5455
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5443-5455
    • Lee, S.J.1    Duong, J.K.2    Stern, D.F.3
  • 35
    • 3542999251 scopus 로고    scopus 로고
    • Cds1 phosphorylation by Rad3-Rad26 kinase is mediated by forkhead-associated domain interaction with Mrc1
    • Tanaka K., and Russell P. Cds1 phosphorylation by Rad3-Rad26 kinase is mediated by forkhead-associated domain interaction with Mrc1. J. Biol. Chem. 279 (2004) 32079-32086
    • (2004) J. Biol. Chem. , vol.279 , pp. 32079-32086
    • Tanaka, K.1    Russell, P.2
  • 37
    • 0033587049 scopus 로고    scopus 로고
    • The BRCT domain of the S. cerevisiae checkpoint protein Rad9 mediates a Rad9-Rad9 interaction after DNA damage
    • Soulier J., and Lowndes N.F. The BRCT domain of the S. cerevisiae checkpoint protein Rad9 mediates a Rad9-Rad9 interaction after DNA damage. Curr. Biol. 9 (1999) 551-554
    • (1999) Curr. Biol. , vol.9 , pp. 551-554
    • Soulier, J.1    Lowndes, N.F.2
  • 38
    • 35548970638 scopus 로고    scopus 로고
    • Rad9 BRCT domain interaction with phosphorylated H2AX regulates the G1 checkpoint in budding yeast
    • Hammet A., Magill C., Heierhorst J., and Jackson S.P. Rad9 BRCT domain interaction with phosphorylated H2AX regulates the G1 checkpoint in budding yeast. EMBO Rep. 8 (2007) 851-857
    • (2007) EMBO Rep. , vol.8 , pp. 851-857
    • Hammet, A.1    Magill, C.2    Heierhorst, J.3    Jackson, S.P.4
  • 40
    • 15444373985 scopus 로고    scopus 로고
    • The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1
    • Giannattasio M., Lazzaro F., Plevani P., and Muzi-Falconi M. The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1. J. Biol. Chem. 280 (2005) 9879-9886
    • (2005) J. Biol. Chem. , vol.280 , pp. 9879-9886
    • Giannattasio, M.1    Lazzaro, F.2    Plevani, P.3    Muzi-Falconi, M.4
  • 41
    • 25444466892 scopus 로고    scopus 로고
    • Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9
    • Wysocki R., Javaheri A., Allard S., Sha F., Cote J., and Kron S.J. Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9. Mol. Cell. Biol. 25 (2005) 8430-8443
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8430-8443
    • Wysocki, R.1    Javaheri, A.2    Allard, S.3    Sha, F.4    Cote, J.5    Kron, S.J.6
  • 43
    • 39749184166 scopus 로고    scopus 로고
    • Phosphorylation of the axial element protein Hop1 by Mec1/Tel1 ensures meiotic interhomolog recombination
    • Carballo J.A., Johnson A.L., Sedgwick S.G., and Cha R.S. Phosphorylation of the axial element protein Hop1 by Mec1/Tel1 ensures meiotic interhomolog recombination. Cell 132 (2008) 758-770
    • (2008) Cell , vol.132 , pp. 758-770
    • Carballo, J.A.1    Johnson, A.L.2    Sedgwick, S.G.3    Cha, R.S.4
  • 44
    • 0037312919 scopus 로고    scopus 로고
    • Direct kinase-to-kinase signaling mediated by the FHA phosphoprotein recognition domain of the Dun1 DNA damage checkpoint kinase
    • Bashkirov V.I., Bashkirova E.V., Haghnazari E., and Heyer W.D. Direct kinase-to-kinase signaling mediated by the FHA phosphoprotein recognition domain of the Dun1 DNA damage checkpoint kinase. Mol. Cell Biol. 23 (2003) 1441-1452
    • (2003) Mol. Cell Biol. , vol.23 , pp. 1441-1452
    • Bashkirov, V.I.1    Bashkirova, E.V.2    Haghnazari, E.3    Heyer, W.D.4
  • 45
    • 33847767159 scopus 로고    scopus 로고
    • Mechanism of Dun1 activation by Rad53 phosphorylation in Saccharomyces cerevisiae
    • Chen S.H., Smolka M.B., and Zhou H. Mechanism of Dun1 activation by Rad53 phosphorylation in Saccharomyces cerevisiae. J. Biol. Chem. 282 (2007) 986-995
    • (2007) J. Biol. Chem. , vol.282 , pp. 986-995
    • Chen, S.H.1    Smolka, M.B.2    Zhou, H.3
  • 46
    • 0037133566 scopus 로고    scopus 로고
    • The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1
    • Zhao X., and Rothstein R. The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 3746-3751
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3746-3751
    • Zhao, X.1    Rothstein, R.2
  • 47
    • 0032161269 scopus 로고    scopus 로고
    • A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools
    • Zhao X., Muller E.G., and Rothstein R. A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools. Mol. Cell 2 (1998) 329-340
    • (1998) Mol. Cell , vol.2 , pp. 329-340
    • Zhao, X.1    Muller, E.G.2    Rothstein, R.3
  • 49
    • 34547499407 scopus 로고    scopus 로고
    • Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases
    • Smolka M.B., Albuquerque C.P., Chen S.H., and Zhou H. Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 10364-10369
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 10364-10369
    • Smolka, M.B.1    Albuquerque, C.P.2    Chen, S.H.3    Zhou, H.4
  • 50
    • 0033527787 scopus 로고    scopus 로고
    • Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms
    • Sanchez Y., Bachant J., Wang H., Hu F., Liu D., Tetzlaff M., and Elledge S.J. Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms. Science 286 (1999) 1166-1171
    • (1999) Science , vol.286 , pp. 1166-1171
    • Sanchez, Y.1    Bachant, J.2    Wang, H.3    Hu, F.4    Liu, D.5    Tetzlaff, M.6    Elledge, S.J.7
  • 51
    • 0242413993 scopus 로고    scopus 로고
    • Two distinct pathways for inhibiting pds1 ubiquitination in response to DNA damage
    • Agarwal R., Tang Z., Yu H., and Cohen-Fix O. Two distinct pathways for inhibiting pds1 ubiquitination in response to DNA damage. J. Biol. Chem. 278 (2003) 45027-45033
    • (2003) J. Biol. Chem. , vol.278 , pp. 45027-45033
    • Agarwal, R.1    Tang, Z.2    Yu, H.3    Cohen-Fix, O.4
  • 52
    • 34447515850 scopus 로고    scopus 로고
    • DNA damage checkpoints inhibit mitotic exit by two different mechanisms
    • Liang F., and Wang Y. DNA damage checkpoints inhibit mitotic exit by two different mechanisms. Mol. Cell Biol. 27 (2007) 5067-5078
    • (2007) Mol. Cell Biol. , vol.27 , pp. 5067-5078
    • Liang, F.1    Wang, Y.2
  • 53
    • 0032254350 scopus 로고    scopus 로고
    • The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation
    • Visintin R., Craig K., Hwang E.S., Prinz S., Tyers M., and Amon A. The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation. Mol. Cell 2 (1998) 709-718
    • (1998) Mol. Cell , vol.2 , pp. 709-718
    • Visintin, R.1    Craig, K.2    Hwang, E.S.3    Prinz, S.4    Tyers, M.5    Amon, A.6
  • 54
    • 33845406202 scopus 로고    scopus 로고
    • The spindle assembly checkpoint regulates the phosphorylation state of a subset of DNA checkpoint proteins in Saccharomyces cerevisiae
    • Clemenson C., and Marsolier-Kergoat M.C. The spindle assembly checkpoint regulates the phosphorylation state of a subset of DNA checkpoint proteins in Saccharomyces cerevisiae. Mol. Cell Biol. 26 (2006) 9149-9161
    • (2006) Mol. Cell Biol. , vol.26 , pp. 9149-9161
    • Clemenson, C.1    Marsolier-Kergoat, M.C.2
  • 55
    • 0344413644 scopus 로고    scopus 로고
    • Cdc7 kinases (DDKs) and checkpoint responses: lessons from two yeasts
    • Duncker B.P., and Brown G.W. Cdc7 kinases (DDKs) and checkpoint responses: lessons from two yeasts. Mutat. Res. 532 (2003) 21-27
    • (2003) Mutat. Res. , vol.532 , pp. 21-27
    • Duncker, B.P.1    Brown, G.W.2
  • 56
    • 0033013124 scopus 로고    scopus 로고
    • Cell cycle regulation of DNA replication initiator factor Dbf4p
    • Cheng L., Collyer T., and Hardy C.F. Cell cycle regulation of DNA replication initiator factor Dbf4p. Mol. Cell Biol. 19 (1999) 4270-4278
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4270-4278
    • Cheng, L.1    Collyer, T.2    Hardy, C.F.3
  • 57
    • 0033215306 scopus 로고    scopus 로고
    • Cdc7p-Dbf4p kinase binds to chromatin during S phase and is regulated by both the APC and the RAD53 checkpoint pathway
    • Weinreich M., and Stillman B. Cdc7p-Dbf4p kinase binds to chromatin during S phase and is regulated by both the APC and the RAD53 checkpoint pathway. EMBO J. 18 (1999) 5334-5346
    • (1999) EMBO J. , vol.18 , pp. 5334-5346
    • Weinreich, M.1    Stillman, B.2
  • 58
    • 41949133033 scopus 로고    scopus 로고
    • The role of the Saccharomyces cerevisiae Cdc7-Dbf4 complex in the replication checkpoint
    • Ogi H., Wang C.Z., Nakai W., Kawasaki Y., and Masumoto H. The role of the Saccharomyces cerevisiae Cdc7-Dbf4 complex in the replication checkpoint. Gene 414 (2008) 32-40
    • (2008) Gene , vol.414 , pp. 32-40
    • Ogi, H.1    Wang, C.Z.2    Nakai, W.3    Kawasaki, Y.4    Masumoto, H.5
  • 59
    • 0034765174 scopus 로고    scopus 로고
    • Regulation of initiation of S phase, replication checkpoint signaling, and maintenance of mitotic chromosome structures during S phase by Hsk1 kinase in the fission yeast
    • Takeda T., Ogino K., Tatebayashi K., Ikeda H., Arai K., and Masai H. Regulation of initiation of S phase, replication checkpoint signaling, and maintenance of mitotic chromosome structures during S phase by Hsk1 kinase in the fission yeast. Mol. Biol. Cell 12 (2001) 1257-1274
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1257-1274
    • Takeda, T.1    Ogino, K.2    Tatebayashi, K.3    Ikeda, H.4    Arai, K.5    Masai, H.6
  • 60
    • 0037115462 scopus 로고    scopus 로고
    • ORC and the intra-S-phase checkpoint: a threshold regulates Rad53p activation in S phase
    • Shimada K., Pasero P., and Gasser S.M. ORC and the intra-S-phase checkpoint: a threshold regulates Rad53p activation in S phase. Genes Dev. 16 (2002) 3236-3252
    • (2002) Genes Dev. , vol.16 , pp. 3236-3252
    • Shimada, K.1    Pasero, P.2    Gasser, S.M.3
  • 61
    • 4644307282 scopus 로고    scopus 로고
    • CDC7/DBF4 functions in the translesion synthesis branch of the RAD6 epistasis group in Saccharomyces cerevisiae
    • Pessoa-Brandao L., and Sclafani R.A. CDC7/DBF4 functions in the translesion synthesis branch of the RAD6 epistasis group in Saccharomyces cerevisiae. Genetics 167 (2004) 1597-1610
    • (2004) Genetics , vol.167 , pp. 1597-1610
    • Pessoa-Brandao, L.1    Sclafani, R.A.2
  • 63
    • 1842472073 scopus 로고    scopus 로고
    • Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage
    • Rouse J. Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage. EMBO J. 23 (2004) 1188-1197
    • (2004) EMBO J. , vol.23 , pp. 1188-1197
    • Rouse, J.1
  • 65
    • 33846088785 scopus 로고    scopus 로고
    • The non-homologous end-joining protein Nej1p is a target of the DNA damage checkpoint
    • Ahnesorg P., and Jackson S.P. The non-homologous end-joining protein Nej1p is a target of the DNA damage checkpoint. DNA Repair (Amst.) 6 (2007) 190-201
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 190-201
    • Ahnesorg, P.1    Jackson, S.P.2
  • 66
    • 33644784811 scopus 로고    scopus 로고
    • Evidence of meiotic crossover control in Saccharomyces cerevisiae through Mec1-mediated phosphorylation of replication protein A
    • Bartrand A.J., Iyasu D., Marinco S.M., and Brush G.S. Evidence of meiotic crossover control in Saccharomyces cerevisiae through Mec1-mediated phosphorylation of replication protein A. Genetics 172 (2006) 27-39
    • (2006) Genetics , vol.172 , pp. 27-39
    • Bartrand, A.J.1    Iyasu, D.2    Marinco, S.M.3    Brush, G.S.4
  • 67
    • 0034307720 scopus 로고    scopus 로고
    • Phosphorylation of the replication protein A large subunit in the Saccharomyces cerevisiae checkpoint response
    • Brush G.S., and Kelly T.J. Phosphorylation of the replication protein A large subunit in the Saccharomyces cerevisiae checkpoint response. Nucleic Acids Res. 28 (2000) 3725-3732
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3725-3732
    • Brush, G.S.1    Kelly, T.J.2
  • 68
    • 0042379940 scopus 로고    scopus 로고
    • Amino acid changes in Xrs2p, Dun1p, and Rfa2p that remove the preferred targets of the ATM family of protein kinases do not affect DNA repair or telomere length in Saccharomyces cerevisiae
    • Mallory J.C., Bashkirov V.I., Trujillo K.M., Solinger J.A., Dominska M., Sung P., Heyer W.D., and Petes T.D. Amino acid changes in Xrs2p, Dun1p, and Rfa2p that remove the preferred targets of the ATM family of protein kinases do not affect DNA repair or telomere length in Saccharomyces cerevisiae. DNA Repair (Amst.) 2 (2003) 1041-1064
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1041-1064
    • Mallory, J.C.1    Bashkirov, V.I.2    Trujillo, K.M.3    Solinger, J.A.4    Dominska, M.5    Sung, P.6    Heyer, W.D.7    Petes, T.D.8
  • 69
    • 0035449349 scopus 로고    scopus 로고
    • The yeast Xrs2 complex functions in S phase checkpoint regulation
    • D'Amours D., and Jackson S.P. The yeast Xrs2 complex functions in S phase checkpoint regulation. Genes Dev. 15 (2001) 2238-2249
    • (2001) Genes Dev. , vol.15 , pp. 2238-2249
    • D'Amours, D.1    Jackson, S.P.2
  • 70
    • 0034513411 scopus 로고    scopus 로고
    • The SOS response: recent insights into umuDC-dependent mutagenesis and DNA damage tolerance
    • Sutton M.D., Smith B.T., Godoy V.G., and Walker G.C. The SOS response: recent insights into umuDC-dependent mutagenesis and DNA damage tolerance. Annu. Rev. Genet. 34 (2000) 479-497
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 479-497
    • Sutton, M.D.1    Smith, B.T.2    Godoy, V.G.3    Walker, G.C.4
  • 73
    • 0038312215 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae chromatin-assembly factors that act during DNA replication function in the maintenance of genome stability
    • Myung K., Pennaneach V., Kats E.S., and Kolodner R.D. Saccharomyces cerevisiae chromatin-assembly factors that act during DNA replication function in the maintenance of genome stability. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 6640-6645
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6640-6645
    • Myung, K.1    Pennaneach, V.2    Kats, E.S.3    Kolodner, R.D.4
  • 74
  • 75
    • 10944233962 scopus 로고    scopus 로고
    • Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair
    • van Attikum H., Fritsch O., Hohn B., and Gasser S.M. Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. Cell 119 (2004) 777-788
    • (2004) Cell , vol.119 , pp. 777-788
    • van Attikum, H.1    Fritsch, O.2    Hohn, B.3    Gasser, S.M.4
  • 76
    • 33748272677 scopus 로고    scopus 로고
    • Interplay between Ino80 and Swr1 chromatin remodeling enzymes regulates cell cycle checkpoint adaptation in response to DNA damage
    • Papamichos-Chronakis M., Krebs J.E., and Peterson C.L. Interplay between Ino80 and Swr1 chromatin remodeling enzymes regulates cell cycle checkpoint adaptation in response to DNA damage. Genes Dev. 20 (2006) 2437-2449
    • (2006) Genes Dev. , vol.20 , pp. 2437-2449
    • Papamichos-Chronakis, M.1    Krebs, J.E.2    Peterson, C.L.3
  • 77
    • 34648834736 scopus 로고    scopus 로고
    • Distinct roles for SWR1 and INO80 chromatin remodeling complexes at chromosomal double-strand breaks
    • van Attikum H., Fritsch O., and Gasser S.M. Distinct roles for SWR1 and INO80 chromatin remodeling complexes at chromosomal double-strand breaks. EMBO J. 26 (2007) 4113-4125
    • (2007) EMBO J. , vol.26 , pp. 4113-4125
    • van Attikum, H.1    Fritsch, O.2    Gasser, S.M.3
  • 78
  • 80
    • 10944232673 scopus 로고    scopus 로고
    • Postreplicative recruitment of cohesin to double-strand breaks is required for DNA repair
    • Strom L., Lindroos H.B., Shirahige K., and Sjogren C. Postreplicative recruitment of cohesin to double-strand breaks is required for DNA repair. Mol. Cell 16 (2004) 1003-1015
    • (2004) Mol. Cell , vol.16 , pp. 1003-1015
    • Strom, L.1    Lindroos, H.B.2    Shirahige, K.3    Sjogren, C.4
  • 81
    • 10944262393 scopus 로고    scopus 로고
    • DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain
    • Unal E., Arbel-Eden A., Sattler U., Shroff R., Lichten M., Haber J.E., and Koshland D. DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain. Mol. Cell 16 (2004) 991-1002
    • (2004) Mol. Cell , vol.16 , pp. 991-1002
    • Unal, E.1    Arbel-Eden, A.2    Sattler, U.3    Shroff, R.4    Lichten, M.5    Haber, J.E.6    Koshland, D.7
  • 82
    • 34447549077 scopus 로고    scopus 로고
    • Postreplicative formation of cohesion is required for repair and induced by a single DNA break
    • Strom L., Karlsson C., Lindroos H.B., Wedahl S., Katou Y., Shirahige K., and Sjogren C. Postreplicative formation of cohesion is required for repair and induced by a single DNA break. Science 317 (2007) 242-245
    • (2007) Science , vol.317 , pp. 242-245
    • Strom, L.1    Karlsson, C.2    Lindroos, H.B.3    Wedahl, S.4    Katou, Y.5    Shirahige, K.6    Sjogren, C.7
  • 83
    • 34447536708 scopus 로고    scopus 로고
    • DNA double-strand breaks trigger genome-wide sister-chromatid cohesion through Eco1 (Ctf7)
    • Unal E., Heidinger-Pauli J.M., and Koshland D. DNA double-strand breaks trigger genome-wide sister-chromatid cohesion through Eco1 (Ctf7). Science 317 (2007) 245-248
    • (2007) Science , vol.317 , pp. 245-248
    • Unal, E.1    Heidinger-Pauli, J.M.2    Koshland, D.3
  • 84
    • 12544256548 scopus 로고    scopus 로고
    • Ctf7p/Eco1p exhibits acetyltransferase activity-but does it matter?
    • Brands A., and Skibbens R.V. Ctf7p/Eco1p exhibits acetyltransferase activity-but does it matter?. Curr. Biol. 15 (2005) R50-51
    • (2005) Curr. Biol. , vol.15
    • Brands, A.1    Skibbens, R.V.2
  • 85
    • 46149118183 scopus 로고    scopus 로고
    • The kleisin subunit of cohesin dictates damage-induced cohesion
    • Heidinger-Pauli J.M., Unal E., Guacci V., and Koshland D. The kleisin subunit of cohesin dictates damage-induced cohesion. Mol. Cell 31 (2008) 47-56
    • (2008) Mol. Cell , vol.31 , pp. 47-56
    • Heidinger-Pauli, J.M.1    Unal, E.2    Guacci, V.3    Koshland, D.4
  • 86
    • 0033635245 scopus 로고    scopus 로고
    • The DNA damage checkpoint signal in budding yeast is nuclear limited
    • Demeter J., Lee S.E., Haber J.E., and Stearns T. The DNA damage checkpoint signal in budding yeast is nuclear limited. Mol. Cell 6 (2000) 487-492
    • (2000) Mol. Cell , vol.6 , pp. 487-492
    • Demeter, J.1    Lee, S.E.2    Haber, J.E.3    Stearns, T.4
  • 87
    • 33845337082 scopus 로고    scopus 로고
    • Checkpoint proteins control morphogenetic events during DNA replication stress in Saccharomyces cerevisiae
    • Enserink J.M., Smolka M.B., Zhou H., and Kolodner R.D. Checkpoint proteins control morphogenetic events during DNA replication stress in Saccharomyces cerevisiae. J. Cell Biol. 175 (2006) 729-741
    • (2006) J. Cell Biol. , vol.175 , pp. 729-741
    • Enserink, J.M.1    Smolka, M.B.2    Zhou, H.3    Kolodner, R.D.4
  • 88
    • 34547420591 scopus 로고    scopus 로고
    • The yeast DNA damage checkpoint proteins control a cytoplasmic response to DNA damage
    • Dotiwala F., Haase J., Arbel-Eden A., Bloom K., and Haber J.E. The yeast DNA damage checkpoint proteins control a cytoplasmic response to DNA damage. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 11358-11363
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 11358-11363
    • Dotiwala, F.1    Haase, J.2    Arbel-Eden, A.3    Bloom, K.4    Haber, J.E.5
  • 89
    • 0035162698 scopus 로고    scopus 로고
    • Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p
    • Gasch A.P., Huang M., Metzner S., Botstein D., Elledge S.J., and Brown P.O. Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p. Mol. Biol. Cell 12 (2001) 2987-3003
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2987-3003
    • Gasch, A.P.1    Huang, M.2    Metzner, S.3    Botstein, D.4    Elledge, S.J.5    Brown, P.O.6
  • 90
    • 0032483576 scopus 로고    scopus 로고
    • The DNA replication and damage checkpoint pathways induce transcription by inhibition of Crt1 repressor
    • Huang M., Zhou Z., and Elledge S.J. The DNA replication and damage checkpoint pathways induce transcription by inhibition of Crt1 repressor. Cell 94 (1998) 595-605
    • (1998) Cell , vol.94 , pp. 595-605
    • Huang, M.1    Zhou, Z.2    Elledge, S.J.3
  • 91
    • 0036464527 scopus 로고    scopus 로고
    • Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase
    • Kim E.M., Jang Y.K., and Park S.D. Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase. Nucleic Acids Res. 30 (2002) 643-648
    • (2002) Nucleic Acids Res. , vol.30 , pp. 643-648
    • Kim, E.M.1    Jang, Y.K.2    Park, S.D.3
  • 92
    • 0034758462 scopus 로고    scopus 로고
    • Two alternative cell cycle checkpoint pathways differentially control DNA damage-dependent induction of MAG1 and DDI1 expression in yeast
    • Zhu Y., and Xiao W. Two alternative cell cycle checkpoint pathways differentially control DNA damage-dependent induction of MAG1 and DDI1 expression in yeast. Mol. Genet. Genomics 266 (2001) 436-444
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 436-444
    • Zhu, Y.1    Xiao, W.2
  • 93
    • 0032401918 scopus 로고    scopus 로고
    • Differential regulation of two closely clustered yeast genes, MAG1 and DDI1, by cell-cycle checkpoints
    • Zhu Y., and Xiao W. Differential regulation of two closely clustered yeast genes, MAG1 and DDI1, by cell-cycle checkpoints. Nucleic Acids Res. 26 (1998) 5402-5408
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5402-5408
    • Zhu, Y.1    Xiao, W.2
  • 94
    • 43049160831 scopus 로고    scopus 로고
    • Rad6-Rad18 mediates a eukaryotic SOS response by ubiquitinating the 9-1-1 checkpoint clamp
    • Fu Y., Zhu Y., Zhang K., Yeung M., Durocher D., and Xiao W. Rad6-Rad18 mediates a eukaryotic SOS response by ubiquitinating the 9-1-1 checkpoint clamp. Cell 133 (2008) 601-611
    • (2008) Cell , vol.133 , pp. 601-611
    • Fu, Y.1    Zhu, Y.2    Zhang, K.3    Yeung, M.4    Durocher, D.5    Xiao, W.6
  • 95
    • 0030664297 scopus 로고    scopus 로고
    • Rad53-dependent phosphorylation of Swi6 and down-regulation of CLN1 and CLN2 transcription occur in response to DNA damage in Saccharomyces cerevisiae
    • Sidorova J.M., and Breeden L.L. Rad53-dependent phosphorylation of Swi6 and down-regulation of CLN1 and CLN2 transcription occur in response to DNA damage in Saccharomyces cerevisiae. Genes Dev. 11 (1997) 3032-3045
    • (1997) Genes Dev. , vol.11 , pp. 3032-3045
    • Sidorova, J.M.1    Breeden, L.L.2
  • 96
    • 0038642063 scopus 로고    scopus 로고
    • Rad53 checkpoint kinase phosphorylation site preference identified in the Swi6 protein of Saccharomyces cerevisiae
    • Sidorova J.M., and Breeden L.L. Rad53 checkpoint kinase phosphorylation site preference identified in the Swi6 protein of Saccharomyces cerevisiae. Mol. Cell Biol. 23 (2003) 3405-3416
    • (2003) Mol. Cell Biol. , vol.23 , pp. 3405-3416
    • Sidorova, J.M.1    Breeden, L.L.2
  • 97
    • 0037172948 scopus 로고    scopus 로고
    • Transcriptional response of Saccharomyces cerevisiae to DNA-damaging agents does not identify the genes that protect against these agents
    • Birrell G.W., Brown J.A., Wu H.I., Giaever G., Chu A.M., Davis R.W., and Brown J.M. Transcriptional response of Saccharomyces cerevisiae to DNA-damaging agents does not identify the genes that protect against these agents. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 8778-8783
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8778-8783
    • Birrell, G.W.1    Brown, J.A.2    Wu, H.I.3    Giaever, G.4    Chu, A.M.5    Davis, R.W.6    Brown, J.M.7
  • 98
    • 0033772765 scopus 로고    scopus 로고
    • Regulatory networks revealed by transcriptional profiling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes
    • Jelinsky S.A., Estep P., Church G.M., and Samson L.D. Regulatory networks revealed by transcriptional profiling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes. Mol. Cell Biol. 20 (2000) 8157-8167
    • (2000) Mol. Cell Biol. , vol.20 , pp. 8157-8167
    • Jelinsky, S.A.1    Estep, P.2    Church, G.M.3    Samson, L.D.4
  • 102
    • 38149130689 scopus 로고    scopus 로고
    • The protein degradation response of Saccharomyces cerevisiae to classical DNA-damaging agents
    • Burgis N.E., and Samson L.D. The protein degradation response of Saccharomyces cerevisiae to classical DNA-damaging agents. Chem. Res. Toxicol. 20 (2007) 1843-1853
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1843-1853
    • Burgis, N.E.1    Samson, L.D.2
  • 103
    • 0030049354 scopus 로고    scopus 로고
    • Radioresistance of Deinococcus radiodurans: functions necessary to survive ionizing radiation are also necessary to survive prolonged desiccation
    • Mattimore V., and Battista J.R. Radioresistance of Deinococcus radiodurans: functions necessary to survive ionizing radiation are also necessary to survive prolonged desiccation. J. Bacteriol. 178 (1996) 633-637
    • (1996) J. Bacteriol. , vol.178 , pp. 633-637
    • Mattimore, V.1    Battista, J.R.2
  • 104
    • 0032530824 scopus 로고    scopus 로고
    • Recovery from DNA replicational stress is the essential function of the S-phase checkpoint pathway
    • Desany B.A., Alcasabas A.A., Bachant J.B., and Elledge S.J. Recovery from DNA replicational stress is the essential function of the S-phase checkpoint pathway. Genes Dev. 12 (1998) 2956-2970
    • (1998) Genes Dev. , vol.12 , pp. 2956-2970
    • Desany, B.A.1    Alcasabas, A.A.2    Bachant, J.B.3    Elledge, S.J.4
  • 105
    • 0035797444 scopus 로고    scopus 로고
    • Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint
    • Tercero J.A., and Diffley J.F. Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint. Nature 412 (2001) 553-557
    • (2001) Nature , vol.412 , pp. 553-557
    • Tercero, J.A.1    Diffley, J.F.2
  • 107
    • 0037178723 scopus 로고    scopus 로고
    • ATR homolog Mec1 promotes fork progression, thus averting breaks in replication slow zones
    • Cha R.S., and Kleckner N. ATR homolog Mec1 promotes fork progression, thus averting breaks in replication slow zones. Science 297 (2002) 602-606
    • (2002) Science , vol.297 , pp. 602-606
    • Cha, R.S.1    Kleckner, N.2
  • 108
    • 0029592020 scopus 로고
    • Dpb11, which interacts with DNA polymerase II(epsilon) in Saccharomyces cerevisiae, has a dual role in S-phase progression and at a cell cycle checkpoint
    • Araki H., Leem S.H., Phongdara A., and Sugino A. Dpb11, which interacts with DNA polymerase II(epsilon) in Saccharomyces cerevisiae, has a dual role in S-phase progression and at a cell cycle checkpoint. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 11791-11795
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11791-11795
    • Araki, H.1    Leem, S.H.2    Phongdara, A.3    Sugino, A.4
  • 110
    • 0030793718 scopus 로고    scopus 로고
    • Rfc5, a replication factor C component, is required for regulation of Rad53 protein kinase in the yeast checkpoint pathway
    • Sugimoto K., Ando S., Shimomura T., and Matsumoto K. Rfc5, a replication factor C component, is required for regulation of Rad53 protein kinase in the yeast checkpoint pathway. Mol. Cell Biol. 17 (1997) 5905-5914
    • (1997) Mol. Cell Biol. , vol.17 , pp. 5905-5914
    • Sugimoto, K.1    Ando, S.2    Shimomura, T.3    Matsumoto, K.4
  • 112
    • 0027968012 scopus 로고
    • The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast
    • Allen J.B., Zhou Z., Siede W., Friedberg E.C., and Elledge S.J. The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast. Genes Dev. 8 (1994) 2401-2415
    • (1994) Genes Dev. , vol.8 , pp. 2401-2415
    • Allen, J.B.1    Zhou, Z.2    Siede, W.3    Friedberg, E.C.4    Elledge, S.J.5
  • 113
    • 0037178740 scopus 로고    scopus 로고
    • Fork reversal and ssDNA accumulation at stalled replication forks owing to checkpoint defects
    • Sogo J.M., Lopes M., and Foiani M. Fork reversal and ssDNA accumulation at stalled replication forks owing to checkpoint defects. Science 297 (2002) 599-602
    • (2002) Science , vol.297 , pp. 599-602
    • Sogo, J.M.1    Lopes, M.2    Foiani, M.3
  • 115
    • 33748905485 scopus 로고    scopus 로고
    • Regulation of DNA replication machinery by Mrc1 in fission yeast
    • Nitani N., Nakamura K., Nakagawa C., Masukata H., and Nakagawa T. Regulation of DNA replication machinery by Mrc1 in fission yeast. Genetics 174 (2006) 155-165
    • (2006) Genetics , vol.174 , pp. 155-165
    • Nitani, N.1    Nakamura, K.2    Nakagawa, C.3    Masukata, H.4    Nakagawa, T.5
  • 116
    • 23944507608 scopus 로고    scopus 로고
    • Molecular anatomy and regulation of a stable replisome at a paused eukaryotic DNA replication fork
    • Calzada A., Hodgson B., Kanemaki M., Bueno A., and Labib K. Molecular anatomy and regulation of a stable replisome at a paused eukaryotic DNA replication fork. Genes Dev. 19 (2005) 1905-1919
    • (2005) Genes Dev. , vol.19 , pp. 1905-1919
    • Calzada, A.1    Hodgson, B.2    Kanemaki, M.3    Bueno, A.4    Labib, K.5
  • 117
    • 33947127410 scopus 로고    scopus 로고
    • Strength in numbers: preventing rereplication via multiple mechanisms in eukaryotic cells
    • Arias E.E., and Walter J.C. Strength in numbers: preventing rereplication via multiple mechanisms in eukaryotic cells. Genes Dev. 21 (2007) 497-518
    • (2007) Genes Dev. , vol.21 , pp. 497-518
    • Arias, E.E.1    Walter, J.C.2
  • 118
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • Labib K., Tercero J.A., and Diffley J.F. Uninterrupted MCM2-7 function required for DNA replication fork progression. Science 288 (2000) 1643-1647
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1    Tercero, J.A.2    Diffley, J.F.3
  • 119
    • 0033988501 scopus 로고    scopus 로고
    • Role of PriA in replication fork reactivation in Escherichia coli
    • Sandler S.J., and Marians K.J. Role of PriA in replication fork reactivation in Escherichia coli. J. Bacteriol. 182 (2000) 9-13
    • (2000) J. Bacteriol. , vol.182 , pp. 9-13
    • Sandler, S.J.1    Marians, K.J.2
  • 121
    • 45549097452 scopus 로고    scopus 로고
    • Positive feedback in cellular control systems
    • Mitrophanov A.Y., and Groisman E.A. Positive feedback in cellular control systems. Bioessays 30 (2008) 542-555
    • (2008) Bioessays , vol.30 , pp. 542-555
    • Mitrophanov, A.Y.1    Groisman, E.A.2
  • 122
    • 47549106474 scopus 로고    scopus 로고
    • Positive feedback of G1 cyclins ensures coherent cell cycle entry
    • Skotheim J.M., Di Talia S., Siggia E.D., and Cross F.R. Positive feedback of G1 cyclins ensures coherent cell cycle entry. Nature 454 (2008) 291-296
    • (2008) Nature , vol.454 , pp. 291-296
    • Skotheim, J.M.1    Di Talia, S.2    Siggia, E.D.3    Cross, F.R.4
  • 123
    • 47549083849 scopus 로고    scopus 로고
    • Positive feedback sharpens the anaphase switch
    • Holt L.J., Krutchinsky A.N., and Morgan D.O. Positive feedback sharpens the anaphase switch. Nature 454 (2008) 353-357
    • (2008) Nature , vol.454 , pp. 353-357
    • Holt, L.J.1    Krutchinsky, A.N.2    Morgan, D.O.3
  • 125
    • 45849117573 scopus 로고    scopus 로고
    • Activation of the cellular DNA damage response in the absence of DNA lesions
    • Soutoglou E., and Misteli T. Activation of the cellular DNA damage response in the absence of DNA lesions. Science 320 (2008) 1507-1510
    • (2008) Science , vol.320 , pp. 1507-1510
    • Soutoglou, E.1    Misteli, T.2
  • 128
    • 0344643062 scopus 로고    scopus 로고
    • PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break
    • Leroy C., Lee S.E., Vaze M.B., Ochsenbien F., Guerois R., Haber J.E., and Marsolier-Kergoat M.C. PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break. Mol. Cell 11 (2003) 827-835
    • (2003) Mol. Cell , vol.11 , pp. 827-835
    • Leroy, C.1    Lee, S.E.2    Vaze, M.B.3    Ochsenbien, F.4    Guerois, R.5    Haber, J.E.6    Marsolier-Kergoat, M.C.7
  • 129
    • 0035105240 scopus 로고    scopus 로고
    • Regulation of Saccharomyces Rad53 checkpoint kinase during adaptation from DNA damage-induced G2/M arrest
    • Pellicioli A., Lee S.E., Lucca C., Foiani M., and Haber J.E. Regulation of Saccharomyces Rad53 checkpoint kinase during adaptation from DNA damage-induced G2/M arrest. Mol. Cell 7 (2001) 293-300
    • (2001) Mol. Cell , vol.7 , pp. 293-300
    • Pellicioli, A.1    Lee, S.E.2    Lucca, C.3    Foiani, M.4    Haber, J.E.5
  • 130
    • 58649097740 scopus 로고    scopus 로고
    • Maintenance of the DNA-damage checkpoint requires DNA-damage-induced mediator protein oligomerization
    • Usui T., Foster S.S., and Petrini J.H. Maintenance of the DNA-damage checkpoint requires DNA-damage-induced mediator protein oligomerization. Mol. Cell 33 (2009) 147-159
    • (2009) Mol. Cell , vol.33 , pp. 147-159
    • Usui, T.1    Foster, S.S.2    Petrini, J.H.3
  • 131
    • 0034964498 scopus 로고    scopus 로고
    • A DNA damage response pathway controlled by Tel1 and the Mre11 complex
    • Usui T., Ogawa H., and Petrini J.H. A DNA damage response pathway controlled by Tel1 and the Mre11 complex. Mol. Cell 7 (2001) 1255-1266
    • (2001) Mol. Cell , vol.7 , pp. 1255-1266
    • Usui, T.1    Ogawa, H.2    Petrini, J.H.3
  • 133
    • 51949118680 scopus 로고    scopus 로고
    • Checkpoint-dependent phosphorylation of Exo1 modulates the DNA damage response
    • Morin I., Ngo H.P., Greenall A., Zubko M.K., Morrice N., and Lydall D. Checkpoint-dependent phosphorylation of Exo1 modulates the DNA damage response. EMBO J. 27 (2008) 2400-2410
    • (2008) EMBO J. , vol.27 , pp. 2400-2410
    • Morin, I.1    Ngo, H.P.2    Greenall, A.3    Zubko, M.K.4    Morrice, N.5    Lydall, D.6
  • 134
    • 0034665462 scopus 로고    scopus 로고
    • Srs2 DNA helicase is involved in checkpoint response and its regulation requires a functional Mec1-dependent pathway and Cdk1 activity
    • Liberi G., Chiolo I., Pellicioli A., Lopes M., Plevani P., Muzi-Falconi M., and Foiani M. Srs2 DNA helicase is involved in checkpoint response and its regulation requires a functional Mec1-dependent pathway and Cdk1 activity. EMBO J. 19 (2000) 5027-5038
    • (2000) EMBO J. , vol.19 , pp. 5027-5038
    • Liberi, G.1    Chiolo, I.2    Pellicioli, A.3    Lopes, M.4    Plevani, P.5    Muzi-Falconi, M.6    Foiani, M.7
  • 135
    • 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. The functions of budding yeast Sae2 in the DNA damage response require Mec1- and Tel1-dependent phosphorylation. Mol. Cell Biol. 24 (2004) 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
  • 136
    • 33845669591 scopus 로고    scopus 로고
    • The telomerase-recruitment domain of the telomere binding protein Cdc13 is regulated by Mec1p/Tel1p-dependent phosphorylation
    • Tseng S.F., Lin J.J., and Teng S.C. The telomerase-recruitment domain of the telomere binding protein Cdc13 is regulated by Mec1p/Tel1p-dependent phosphorylation. Nucleic Acids Res. 34 (2006) 6327-6336
    • (2006) Nucleic Acids Res. , vol.34 , pp. 6327-6336
    • Tseng, S.F.1    Lin, J.J.2    Teng, S.C.3
  • 137
    • 33845991538 scopus 로고    scopus 로고
    • RPA2 is a direct downstream target for ATR to regulate the S-phase checkpoint
    • Olson E., Nievera C.J., Klimovich V., Fanning E., and Wu X. RPA2 is a direct downstream target for ATR to regulate the S-phase checkpoint. J. Biol. Chem. 281 (2006) 39517-39533
    • (2006) J. Biol. Chem. , vol.281 , pp. 39517-39533
    • Olson, E.1    Nievera, C.J.2    Klimovich, V.3    Fanning, E.4    Wu, X.5


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