메뉴 건너뛰기




Volumn 43, Issue 10, 2015, Pages 4990-5001

The amino-terminal tails of histones H2A and H3 coordinate efficient base excision repair, DNA damage signaling and postreplication repair in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA GLYCOSYLTRANSFERASE; FUNGAL ENZYME; HISTONE H2A; HISTONE H3; MAG1 PROTEIN; MESYLIC ACID METHYL ESTER; PROTEIN RAD9; RAD18 PROTEIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; HISTONE; MAG1 PROTEIN, S CEREVISIAE; RAD18 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84931275589     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv372     Document Type: Article
Times cited : (11)

References (63)
  • 2
    • 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. (2001) Recruitment of Mec1 and Ddc1 checkpoint proteins to double-strand breaks through distinct mechanisms. Science, 294, 867-870.
    • (2001) Science , vol.294 , pp. 867-870
    • Kondo, T.1    Wakayama, T.2    Naiki, T.3    Matsumoto, K.4    Sugimoto, K.5
  • 3
    • 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. (2001) Two checkpoint complexes are independently recruited to sites of DNA damage in vivo. Genes Dev., 15, 2809-2821.
    • (2001) Genes Dev. , vol.15 , pp. 2809-2821
    • Melo, J.A.1    Cohen, J.2    Toczyski, D.P.3
  • 4
    • 24944575222 scopus 로고    scopus 로고
    • Signal transduction: How rad53 kinase is activated
    • Pellicioli, A. and Foiani, M. (2005) Signal transduction: how rad53 kinase is activated. Curr. Biol., 15, R769-R771.
    • (2005) Curr. Biol. , vol.15 , pp. R769-R771
    • Pellicioli, A.1    Foiani, M.2
  • 5
    • 33746816108 scopus 로고    scopus 로고
    • The Rad53 signal transduction pathway: Replication fork stabilization, DNA repair, and adaptation
    • Branzei, D. and Foiani, M. (2006) The Rad53 signal transduction pathway: replication fork stabilization, DNA repair, and adaptation. Exp. Cell Res., 312, 2654-2659.
    • (2006) Exp. Cell Res. , vol.312 , pp. 2654-2659
    • Branzei, D.1    Foiani, M.2
  • 6
    • 84876162526 scopus 로고    scopus 로고
    • The DNA damage checkpoint response to replication stress: A Game of Forks
    • Jossen, R. and Bermejo, R. (2013) The DNA damage checkpoint response to replication stress: a Game of Forks. Front. Genet., 4, 26.
    • (2013) Front. Genet. , vol.4 , pp. 26
    • Jossen, R.1    Bermejo, R.2
  • 8
    • 80052702417 scopus 로고    scopus 로고
    • Timing and spacing of ubiquitin-dependent DNA damage bypass
    • Ulrich, H.D. (2011) Timing and spacing of ubiquitin-dependent DNA damage bypass. FEBS Lett., 585, 2861-2867.
    • (2011) FEBS Lett. , vol.585 , pp. 2861-2867
    • Ulrich, H.D.1
  • 9
    • 84863001577 scopus 로고    scopus 로고
    • Prime, repair, restore: The active role of chromatin in the DNA damage response
    • Soria, G., Polo, S.E. and Almouzni, G. (2012) Prime, repair, restore: the active role of chromatin in the DNA damage response. Mol. Cell, 46, 722-734.
    • (2012) Mol. Cell , vol.46 , pp. 722-734
    • Soria, G.1    Polo, S.E.2    Almouzni, G.3
  • 10
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F. and Richmond, T.J. (1997) Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature, 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 11
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White, C.L., Suto, R.K. and Luger, K. (2001) Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J., 20, 5207-5218.
    • (2001) EMBO J. , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 12
    • 0038605538 scopus 로고    scopus 로고
    • Intra-and inter-nucleosomal protein-DNA interactions of the core histone tail domains in a model system
    • Zheng, C. and Hayes, J.J. (2003) Intra-and inter-nucleosomal protein-DNA interactions of the core histone tail domains in a model system. J. Biol. Chem., 278, 24217-24224.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24217-24224
    • Zheng, C.1    Hayes, J.J.2
  • 13
    • 84897475985 scopus 로고    scopus 로고
    • Intra-and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure
    • Pepenella, S., Murphy, K.J. and Hayes, J.J. (2013) Intra-and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure. Chromosoma, 123, 3-13.
    • (2013) Chromosoma , vol.123 , pp. 3-13
    • Pepenella, S.1    Murphy, K.J.2    Hayes, J.J.3
  • 14
    • 0022500042 scopus 로고
    • Yeast histone H2A and H2B amino termini have interchangeable functions
    • Schuster, T., Han, M. and Grunstein, M. (1986) Yeast histone H2A and H2B amino termini have interchangeable functions. Cell, 45, 445-451.
    • (1986) Cell , vol.45 , pp. 445-451
    • Schuster, T.1    Han, M.2    Grunstein, M.3
  • 15
    • 0025880340 scopus 로고
    • The highly conserved N-terminal domains of histones H3 and H4 are required for normal cell cycle progression
    • Morgan, B.A., Mittman, B.A. and Smith, M.M. (1991) The highly conserved N-terminal domains of histones H3 and H4 are required for normal cell cycle progression. Mol. Cell. Biol., 11, 4111-4120.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4111-4120
    • Morgan, B.A.1    Mittman, B.A.2    Smith, M.M.3
  • 16
    • 84859579664 scopus 로고    scopus 로고
    • Mutagenesis of pairwise combinations of histone amino-terminal tails reveals functional redundancy in budding yeast
    • Kim, J.A., Hsu, J.Y., Smith, M.M. and Allis, C.D. (2012) Mutagenesis of pairwise combinations of histone amino-terminal tails reveals functional redundancy in budding yeast. Proc. Natl. Acad. Sci. U. S. A., 109, 5779-5784.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5779-5784
    • Kim, J.A.1    Hsu, J.Y.2    Smith, M.M.3    Allis, C.D.4
  • 17
    • 0023011595 scopus 로고
    • Changes in nuclear protein acetylation in UV-damaged human cells
    • Ramanathan, B. and Smerdon, M.J. (1986) Changes in nuclear protein acetylation in UV-damaged human cells. Carcinogenesis, 7, 1087-1094.
    • (1986) Carcinogenesis , vol.7 , pp. 1087-1094
    • Ramanathan, B.1    Smerdon, M.J.2
  • 18
    • 20844453256 scopus 로고    scopus 로고
    • UV irradiation stimulates histone acetylation and chromatin remodeling at a repressed yeast locus
    • Yu, Y., Teng, Y., Liu, H., Reed, S.H. and Waters, R. (2005) UV irradiation stimulates histone acetylation and chromatin remodeling at a repressed yeast locus. Proc Natl. Acad. Sci. U.S.A., 102, 8650-8655.
    • (2005) Proc Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8650-8655
    • Yu, Y.1    Teng, Y.2    Liu, H.3    Reed, S.H.4    Waters, R.5
  • 20
    • 33749520485 scopus 로고    scopus 로고
    • Rad4-Rad23 interaction with SWI/SNF links ATP-dependent chromatin remodeling with nucleotide excision repair
    • Gong, F., Fahy, D. and Smerdon, M.J. (2006) Rad4-Rad23 interaction with SWI/SNF links ATP-dependent chromatin remodeling with nucleotide excision repair. Nat. Struct. Mol. Biol., 13, 902-907.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 902-907
    • Gong, F.1    Fahy, D.2    Smerdon, M.J.3
  • 21
    • 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. (2005) Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9. Mol. Cell. Biol., 25, 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
  • 22
    • 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 Falconi, M.M. (2005) The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1. J. Biol. Chem., 280, 9879-9886.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9879-9886
    • Giannattasio, M.1    Lazzaro, F.2    Plevani, P.3    Falconi, M.M.4
  • 23
    • 0033617334 scopus 로고    scopus 로고
    • Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle-and developmentally regulated promoter
    • Cosma, M.P., Tanaka, T. and Nasmyth, K. (1999) Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle-and developmentally regulated promoter. Cell, 97, 299-311.
    • (1999) Cell , vol.97 , pp. 299-311
    • Cosma, M.P.1    Tanaka, T.2    Nasmyth, K.3
  • 26
    • 77955982287 scopus 로고    scopus 로고
    • Profcient repair in chromatin remodeling defective ino80 mutants of Saccharomyces cerevisiae highlights replication defects as the main contributor to DNA damage sensitivity
    • Czaja, W., Bespalov, V.A., Hinz, J.M. and Smerdon, M.J. (2010) Profcient repair in chromatin remodeling defective ino80 mutants of Saccharomyces cerevisiae highlights replication defects as the main contributor to DNA damage sensitivity. DNA Repair, 9, 976-984.
    • (2010) DNA Repair , vol.9 , pp. 976-984
    • Czaja, W.1    Bespalov, V.A.2    Hinz, J.M.3    Smerdon, M.J.4
  • 27
    • 0035167353 scopus 로고    scopus 로고
    • Improved method for measuring the ensemble average of strand breaks in genomic DNA
    • Bespalov, V.A., Conconi, A., Zhang, X., Fahy, D. and Smerdon, M.J. (2001) Improved method for measuring the ensemble average of strand breaks in genomic DNA. Environ. Mol. Mutagen., 38, 166-174.
    • (2001) Environ. Mol. Mutagen. , vol.38 , pp. 166-174
    • Bespalov, V.A.1    Conconi, A.2    Zhang, X.3    Fahy, D.4    Smerdon, M.J.5
  • 28
    • 46349089093 scopus 로고    scopus 로고
    • A single amino acid change in histone H4 enhances UV survival and DNA repair in yeast
    • Nag, R., Gong, F., Fahy, D. and Smerdon, M.J. (2008) A single amino acid change in histone H4 enhances UV survival and DNA repair in yeast. Nucleic Acids Res., 36, 3857-3866.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3857-3866
    • Nag, R.1    Gong, F.2    Fahy, D.3    Smerdon, M.J.4
  • 29
    • 79955964337 scopus 로고    scopus 로고
    • Evidence that the histone methyltransferase Dot1 mediates global genomic repair by methylating histone H3 on lysine 79
    • Tatum, D. and Li, S.S. (2011) Evidence that the histone methyltransferase Dot1 mediates global genomic repair by methylating histone H3 on lysine 79. J. Biol. Chem., 286, 17530-17535.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17530-17535
    • Tatum, D.1    Li, S.S.2
  • 30
    • 0037160120 scopus 로고    scopus 로고
    • Nucleosome structure and repair of N-methylpurines in the GAL1-10 genes of Saccharomyces cerevisiae
    • Li, S. and Smerdon, M.J. (2002) Nucleosome structure and repair of N-methylpurines in the GAL1-10 genes of Saccharomyces cerevisiae. J. Biol. Chem., 277, 44651-44659.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44651-44659
    • Li, S.1    Smerdon, M.J.2
  • 31
    • 0034429854 scopus 로고    scopus 로고
    • Low-and high-resolution mapping of DNA damage at specifc sites
    • Li, S., Waters, R. and Smerdon, M.J. (2000) Low-and high-resolution mapping of DNA damage at specifc sites. Methods, 22, 170-179.
    • (2000) Methods , vol.22 , pp. 170-179
    • Li, S.1    Waters, R.2    Smerdon, M.J.3
  • 32
    • 51549087123 scopus 로고    scopus 로고
    • Probing nucleosome function: A highly versatile library of synthetic histone H3 and H4 mutants
    • Dai, J., Hyland, E.M., Yuan, D.S., Huang, H., Bader, J.S. and Boeke, J.D. (2008) Probing nucleosome function: a highly versatile library of synthetic histone H3 and H4 mutants. Cell, 134, 1066-1078.
    • (2008) Cell , vol.134 , pp. 1066-1078
    • Dai, J.1    Hyland, E.M.2    Yuan, D.S.3    Huang, H.4    Bader, J.S.5    Boeke, J.D.6
  • 33
    • 0036888874 scopus 로고    scopus 로고
    • Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair
    • Qin, S. and Parthun, M.R. (2002) Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair. Mol. Cell. Biol., 22, 8353-8365.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8353-8365
    • Qin, S.1    Parthun, M.R.2
  • 34
    • 75349098018 scopus 로고    scopus 로고
    • A compiled and systematic reference map of nucleosome positions across the Saccharomyces cerevisiae genome
    • Jiang, C. and Pugh, B.F. (2009) A compiled and systematic reference map of nucleosome positions across the Saccharomyces cerevisiae genome. Genome Biol., 10, R109.
    • (2009) Genome Biol. , vol.10 , pp. R109
    • Jiang, C.1    Pugh, B.F.2
  • 36
    • 0004732033 scopus 로고
    • Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli
    • Chen, J., Derfer, B., Maskati, A. and Samson, L. (1989) Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A., 86, 7961-7965.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7961-7965
    • Chen, J.1    Derfer, B.2    Maskati, A.3    Samson, L.4
  • 38
    • 0029085781 scopus 로고
    • A checkpoint regulates the rate of progression through S phase in S. Cerevisiae in response to DNA damage
    • Paulovich, A.G. and Hartwell, L.H. (1995) A checkpoint regulates the rate of progression through S phase in S. cerevisiae in response to DNA damage. Cell, 82, 841-847.
    • (1995) Cell , vol.82 , pp. 841-847
    • Paulovich, A.G.1    Hartwell, L.H.2
  • 39
    • 0037328929 scopus 로고    scopus 로고
    • Role of the Saccharomyces cerevisiae Rad9 protein in sensing and responding to DNA damage
    • Toh, G.W. and Lowndes, N.F. (2003) Role of the Saccharomyces cerevisiae Rad9 protein in sensing and responding to DNA damage. Biochem. Soc. Trans., 31, 242-246.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 242-246
    • Toh, G.W.1    Lowndes, N.F.2
  • 40
    • 1242351988 scopus 로고    scopus 로고
    • A domain of Rad9 specifcally required for activation of Chk1 in budding yeast
    • Blankley, R.T. and Lydall, D. (2004) A domain of Rad9 specifcally required for activation of Chk1 in budding yeast. J. Cell Sci., 117, 601-608.
    • (2004) J. Cell Sci. , vol.117 , pp. 601-608
    • Blankley, R.T.1    Lydall, D.2
  • 41
    • 23244444605 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Rad9 acts as a Mec1 adaptor to allow Rad53 activation
    • Sweeney, F.D., Yang, F., Chi, A., Shabanowitz, J., Hunt, D.F. and Durocher, D. (2005) Saccharomyces cerevisiae Rad9 acts as a Mec1 adaptor to allow Rad53 activation. Curr. Biol., 15, 1364-1375.
    • (2005) Curr. Biol. , vol.15 , pp. 1364-1375
    • Sweeney, F.D.1    Yang, F.2    Chi, A.3    Shabanowitz, J.4    Hunt, D.F.5    Durocher, D.6
  • 42
    • 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. (2008) Rad6-Rad18 mediates a eukaryotic SOS response by ubiquitinating the 9-1-1 checkpoint clamp. Cell, 133, 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
  • 43
    • 33845735505 scopus 로고    scopus 로고
    • DNA damage checkpoints are involved in postreplication repair
    • Barbour, L., Ball, L.G., Zhang, K. and Xiao, W. (2006) DNA damage checkpoints are involved in postreplication repair. Genetics, 174, 1789-1800.
    • (2006) Genetics , vol.174 , pp. 1789-1800
    • Barbour, L.1    Ball, L.G.2    Zhang, K.3    Xiao, W.4
  • 44
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk, K., Recht, J. and Osley, M.A. (2000) Rad6-dependent ubiquitination of histone H2B in yeast. Science, 287, 501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 46
    • 0030800865 scopus 로고    scopus 로고
    • Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities
    • Bailly, V., Lauder, S., Prakash, S. and Prakash, L. (1997) Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J. Biol. Chem., 272, 23360-23365.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23360-23365
    • Bailly, V.1    Lauder, S.2    Prakash, S.3    Prakash, L.4
  • 47
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modifcation 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 modifcation 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
  • 48
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel, B., Wunning, I. and Varshavsky, A. (1990) The recognition component of the N-end rule pathway. EMBO J., 9, 3179-3189.
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wunning, I.2    Varshavsky, A.3
  • 49
    • 38949119689 scopus 로고    scopus 로고
    • Genome-wide analysis identifes MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation
    • Ju, D., Wang, X., Xu, H. and Xie, Y. (2008) Genome-wide analysis identifes MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation. Mol. Cell. Biol., 28, 1404-1412.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1404-1412
    • Ju, D.1    Wang, X.2    Xu, H.3    Xie, Y.4
  • 50
    • 33644778778 scopus 로고    scopus 로고
    • A DNA integrity network in the yeast Saccharomyces cerevisiae
    • Pan, X., Ye, P., Yuan, D.S., Wang, X., Bader, J.S. and Boeke, J.D. (2006) A DNA integrity network in the yeast Saccharomyces cerevisiae. Cell, 124, 1069-1081.
    • (2006) Cell , vol.124 , pp. 1069-1081
    • Pan, X.1    Ye, P.2    Yuan, D.S.3    Wang, X.4    Bader, J.S.5    Boeke, J.D.6
  • 51
    • 84876398399 scopus 로고    scopus 로고
    • DNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiae
    • Boiteux, S. and Jinks-Robertson, S. (2013) DNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiae. Genetics, 193, 1025-1064.
    • (2013) Genetics , vol.193 , pp. 1025-1064
    • Boiteux, S.1    Jinks-Robertson, S.2
  • 52
    • 0017497959 scopus 로고
    • The biological effects and mode of action of L-canavanine, a structural analogue of L-arginine
    • Rosenthal, G.A. (1977) The biological effects and mode of action of L-canavanine, a structural analogue of L-arginine. Q. Rev. Biol., 52, 155-178.
    • (1977) Q. Rev. Biol. , vol.52 , pp. 155-178
    • Rosenthal, G.A.1
  • 53
    • 0033573938 scopus 로고    scopus 로고
    • Global response of Saccharomyces cerevisiae to an alkylating agent
    • Jelinsky, S.A. and Samson, L.D. (1999) Global response of Saccharomyces cerevisiae to an alkylating agent. Proc. Natl. Acad. Sci. U.S.A., 96, 1486-1491.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1486-1491
    • Jelinsky, S.A.1    Samson, L.D.2
  • 54
    • 53749086073 scopus 로고    scopus 로고
    • DNA damage-induced gene expression in Saccharomyces cerevisiae
    • Fu, Y., Pastushok, L. and Xiao, W. (2008) DNA damage-induced gene expression in Saccharomyces cerevisiae. FEMS Microbiol. Rev., 32, 908-926.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 908-926
    • Fu, Y.1    Pastushok, L.2    Xiao, W.3
  • 55
    • 84883489451 scopus 로고    scopus 로고
    • Proteasome inhibition enhances resistance to DNA damage via upregulation of Rpn4-dependent DNA repair genes
    • Karpov, D.S., Spasskaya, D.S., Tutyaeva, V.V., Mironov, A.S. and Karpov, V.L. (2013) Proteasome inhibition enhances resistance to DNA damage via upregulation of Rpn4-dependent DNA repair genes. Febs Lett., 587, 3108-3114.
    • (2013) Febs Lett. , vol.587 , pp. 3108-3114
    • Karpov, D.S.1    Spasskaya, D.S.2    Tutyaeva, V.V.3    Mironov, A.S.4    Karpov, V.L.5
  • 56
    • 4844219971 scopus 로고    scopus 로고
    • Pdr3 is required for DNA damage induction of MAG1 and DDI1 via a bi-directional promoter element
    • Zhu, Y. and Xiao, W. (2004) Pdr3 is required for DNA damage induction of MAG1 and DDI1 via a bi-directional promoter element. Nucleic Acids Res., 32, 5066-5075.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5066-5075
    • Zhu, Y.1    Xiao, W.2
  • 57
    • 0027359370 scopus 로고
    • A common element involved in transcriptional regulation of two DNA alkylation repair genes (MAG and MGT1) of Saccharomyces cerevisiae
    • Xiao, W., Singh, K.K., Chen, B. and Samson, L. (1993) A common element involved in transcriptional regulation of two DNA alkylation repair genes (MAG and MGT1) of Saccharomyces cerevisiae. Mol. Cell. Biol., 13, 7213-7221.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7213-7221
    • Xiao, W.1    Singh, K.K.2    Chen, B.3    Samson, L.4
  • 58
    • 0033772765 scopus 로고    scopus 로고
    • Regulatory networks revealed by transcriptional profling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes
    • Jelinsky, S.A., Estep, P., Church, G.M. and Samson, L.D. (2000) Regulatory networks revealed by transcriptional profling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes. Mol. Cell. Biol., 20, 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
  • 59
    • 33748807217 scopus 로고    scopus 로고
    • Yeast G1 DNA damage checkpoint regulation by H2A phosphorylation is independent of chromatin remodeling
    • Javaheri, A., Wysocki, R., Jobin-Robitaille, O., Altaf, M., Cote, J. and Kron, S.J. (2006) Yeast G1 DNA damage checkpoint regulation by H2A phosphorylation is independent of chromatin remodeling. Proc. Natl. Acad. Sci. U.S.A., 103, 13771-13776.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 13771-13776
    • Javaheri, A.1    Wysocki, R.2    Jobin-Robitaille, O.3    Altaf, M.4    Cote, J.5    Kron, S.J.6
  • 60
    • 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. (1998) Differential regulation of two closely clustered yeast genes, MAG1 and DDI1, by cell-cycle checkpoints. Nucleic Acids Res., 26, 5402-5408.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5402-5408
    • Zhu, Y.1    Xiao, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.