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Volumn 55, Issue 6, 2014, Pages 818-828

NuA4 Initiates Dynamic Histone H4 Acetylation to Promote High-Fidelity Sister Chromatid Recombination at Postreplication Gaps

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE SIR2; HISTONE H4; LYSINE; MESYLIC ACID METHYL ESTER; PROTEIN; PROTEIN HAT1; PROTEIN HOS2; PROTEIN HST1; PROTEIN NUA4; RAD5 PROTEIN; RAD52 PROTEIN; RAD57 PROTEIN; REPETITIVE DNA; UNCLASSIFIED DRUG; HISTONE; NUA4 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84908020488     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.07.007     Document Type: Article
Times cited : (42)

References (58)
  • 1
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard S., Utley R.T., Savard J., Clarke A., Grant P., Brandl C.J., Pillus L., Workman J.L., CÔté J. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J. 1999, 18:5108-5119.
    • (1999) EMBO J. , vol.18 , pp. 5108-5119
    • Allard, S.1    Utley, R.T.2    Savard, J.3    Clarke, A.4    Grant, P.5    Brandl, C.J.6    Pillus, L.7    Workman, J.L.8    Côté, J.9
  • 3
    • 39749128389 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation for determining the association ofproteins with specific genomic sequences invivo
    • 69:21.3:21.3.1-21.3.33
    • Aparicio O., Geisberg J.V., Sekinger E., Yang A., Moqtaderi Z., Struhl K. Chromatin immunoprecipitation for determining the association ofproteins with specific genomic sequences invivo. Curr. Protoc. Mol. Biol. 2005, 69:21.3:21.3.1-21.3.33.
    • (2005) Curr. Protoc. Mol. Biol.
    • Aparicio, O.1    Geisberg, J.V.2    Sekinger, E.3    Yang, A.4    Moqtaderi, Z.5    Struhl, K.6
  • 4
    • 79959947909 scopus 로고    scopus 로고
    • Chromatin response to DNA double-strand break damage
    • Bao Y. Chromatin response to DNA double-strand break damage. Epigenomics 2011, 3:307-321.
    • (2011) Epigenomics , vol.3 , pp. 307-321
    • Bao, Y.1
  • 5
    • 84885373715 scopus 로고    scopus 로고
    • DNA repair choice defines a common pathway for recruitment of chromatin regulators
    • Bennett G., Papamichos-Chronakis M., Peterson C.L. DNA repair choice defines a common pathway for recruitment of chromatin regulators. Nat. Commun. 2013, 4:2084.
    • (2013) Nat. Commun. , vol.4 , pp. 2084
    • Bennett, G.1    Papamichos-Chronakis, M.2    Peterson, C.L.3
  • 7
    • 84857136872 scopus 로고    scopus 로고
    • The two different isoforms of the RSC chromatin remodeling complex play distinct roles in DNA damage responses
    • Chambers A.L., Brownlee P.M., Durley S.C., Beacham T., Kent N.A., Downs J.A. The two different isoforms of the RSC chromatin remodeling complex play distinct roles in DNA damage responses. PLoS ONE 2012, 7:e32016.
    • (2012) PLoS ONE , vol.7 , pp. e32016
    • Chambers, A.L.1    Brownlee, P.M.2    Durley, S.C.3    Beacham, T.4    Kent, N.A.5    Downs, J.A.6
  • 9
    • 0036889332 scopus 로고    scopus 로고
    • NuA4 subunit Yng2 function in intra-S-phase DNA damage response
    • Choy J.S., Kron S.J. NuA4 subunit Yng2 function in intra-S-phase DNA damage response. Mol. Cell. Biol. 2002, 22:8215-8225.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8215-8225
    • Choy, J.S.1    Kron, S.J.2
  • 10
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol. Cell. Biol. 1999, 19:2515-2526.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2515-2526
    • Clarke, A.S.1    Lowell, J.E.2    Jacobson, S.J.3    Pillus, L.4
  • 11
    • 33845785225 scopus 로고    scopus 로고
    • Postreplication repair inhibits CAG.CTG repeat expansions in Saccharomyces cerevisiae
    • Daee D.L., Mertz T., Lahue R.S. Postreplication repair inhibits CAG.CTG repeat expansions in Saccharomyces cerevisiae. Mol. Cell. Biol. 2007, 27:102-110.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 102-110
    • Daee, D.L.1    Mertz, T.2    Lahue, R.S.3
  • 14
    • 0034922586 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae rad51 mutants are defective in DNA damage-associated sister chromatid exchanges but exhibit increased rates of homology-directed translocations
    • Fasullo M., Giallanza P., Dong Z., Cera C., Bennett T. Saccharomyces cerevisiae rad51 mutants are defective in DNA damage-associated sister chromatid exchanges but exhibit increased rates of homology-directed translocations. Genetics 2001, 158:959-972.
    • (2001) Genetics , vol.158 , pp. 959-972
    • Fasullo, M.1    Giallanza, P.2    Dong, Z.3    Cera, C.4    Bennett, T.5
  • 17
    • 34547681831 scopus 로고    scopus 로고
    • Chromosome fragility: molecular mechanisms and cellular consequences
    • Freudenreich C.H. Chromosome fragility: molecular mechanisms and cellular consequences. Front. Biosci. 2007, 12:4911-4924.
    • (2007) Front. Biosci. , vol.12 , pp. 4911-4924
    • Freudenreich, C.H.1
  • 18
    • 84863131927 scopus 로고    scopus 로고
    • The double-bromodomain proteins Bdf1 and Bdf2 modulate chromatin structure to regulate S-phase stress response in S. pombe
    • Garabedian M.V., Noguchi C., Ziegler M.A., Mukund M.D., Singh T., Nakamura T., Noguchi E., et al. The double-bromodomain proteins Bdf1 and Bdf2 modulate chromatin structure to regulate S-phase stress response in S. pombe. Genetics 2012, 190:487-500.
    • (2012) Genetics , vol.190 , pp. 487-500
    • Garabedian, M.V.1    Noguchi, C.2    Ziegler, M.A.3    Mukund, M.D.4    Singh, T.5    Nakamura, T.6    Noguchi, E.7
  • 19
    • 79952272536 scopus 로고    scopus 로고
    • New functions of Ctf18-RFC in preserving genome stability outside its role in sister chromatid cohesion
    • Gellon L., Razidlo D.F., Gleeson O., Verra L., Schulz D., Lahue R.S., Freudenreich C.H. New functions of Ctf18-RFC in preserving genome stability outside its role in sister chromatid cohesion. PLoS Genet. 2011, 7:e1001298.
    • (2011) PLoS Genet. , vol.7 , pp. e1001298
    • Gellon, L.1    Razidlo, D.F.2    Gleeson, O.3    Verra, L.4    Schulz, D.5    Lahue, R.S.6    Freudenreich, C.H.7
  • 21
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • Kimura A., Umehara T., Horikoshi M. Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing. Nat. Genet. 2002, 32:370-377.
    • (2002) Nat. Genet. , vol.32 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 22
    • 79961083402 scopus 로고    scopus 로고
    • Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice
    • Krishnan V., Chow M.Z., Wang Z., Zhang L., Liu B., Liu X., Zhou Z. Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice. Proc. Natl. Acad. Sci. USA 2011, 108:12325-12330.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 12325-12330
    • Krishnan, V.1    Chow, M.Z.2    Wang, Z.3    Zhang, L.4    Liu, B.5    Liu, X.6    Zhou, Z.7
  • 23
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • Kurdistani S.K., Tavazoie S., Grunstein M. Mapping global histone acetylation patterns to gene expression. Cell 2004, 117:721-733.
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 24
    • 78649533191 scopus 로고    scopus 로고
    • MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1
    • Li X., Corsa C.A., Pan P.W., Wu L., Ferguson D., Yu X., Min J., Dou Y. MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1. Mol. Cell. Biol. 2010, 30:5335-5347.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5335-5347
    • Li, X.1    Corsa, C.A.2    Pan, P.W.3    Wu, L.4    Ferguson, D.5    Yu, X.6    Min, J.7    Dou, Y.8
  • 25
    • 48749114997 scopus 로고    scopus 로고
    • A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation
    • Lin Y.Y., Qi Y., Lu J.Y., Pan X., Yuan D.S., Zhao Y., Bader J.S., Boeke J.D. A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation. Genes Dev. 2008, 22:2062-2074.
    • (2008) Genes Dev. , vol.22 , pp. 2062-2074
    • Lin, Y.Y.1    Qi, Y.2    Lu, J.Y.3    Pan, X.4    Yuan, D.S.5    Zhao, Y.6    Bader, J.S.7    Boeke, J.D.8
  • 26
    • 0034106128 scopus 로고    scopus 로고
    • Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities
    • Loewith R., Meijer M., Lees-Miller S.P., Riabowol K., Young D. Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol. Cell. Biol. 2000, 20:3807-3816.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3807-3816
    • Loewith, R.1    Meijer, M.2    Lees-Miller, S.P.3    Riabowol, K.4    Young, D.5
  • 27
    • 0032499747 scopus 로고    scopus 로고
    • Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast
    • Ma X.J., Wu J., Altheim B.A., Schultz M.C., Grunstein M. Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast. Proc. Natl. Acad. Sci. USA 1998, 95:6693-6698.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6693-6698
    • Ma, X.J.1    Wu, J.2    Altheim, B.A.3    Schultz, M.C.4    Grunstein, M.5
  • 28
    • 77958109197 scopus 로고    scopus 로고
    • Mechanisms of trinucleotide repeat instability during human development
    • McMurray C.T. Mechanisms of trinucleotide repeat instability during human development. Nat. Rev. Genet. 2010, 11:786-799.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 786-799
    • McMurray, C.T.1
  • 29
    • 33747609801 scopus 로고    scopus 로고
    • Genome-wide patterns of histone modifications in yeast
    • Millar C.B., Grunstein M. Genome-wide patterns of histone modifications in yeast. Nat. Rev. Mol. Cell Biol. 2006, 7:657-666.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 657-666
    • Millar, C.B.1    Grunstein, M.2
  • 30
    • 23044489367 scopus 로고    scopus 로고
    • Acetylation of yeast histone H4 lysine 16: a switch for protein interactions in heterochromatin and euchromatin
    • Millar C.B., Kurdistani S.K., Grunstein M. Acetylation of yeast histone H4 lysine 16: a switch for protein interactions in heterochromatin and euchromatin. Cold Spring Harb. Symp. Quant. Biol. 2004, 69:193-200.
    • (2004) Cold Spring Harb. Symp. Quant. Biol. , vol.69 , pp. 193-200
    • Millar, C.B.1    Kurdistani, S.K.2    Grunstein, M.3
  • 31
    • 77953085206 scopus 로고    scopus 로고
    • Multiple Rad5 activities mediate sister chromatid recombination to bypass DNA damage at stalled replication forks
    • Minca E.C., Kowalski D. Multiple Rad5 activities mediate sister chromatid recombination to bypass DNA damage at stalled replication forks. Mol. Cell 2010, 38:649-661.
    • (2010) Mol. Cell , vol.38 , pp. 649-661
    • Minca, E.C.1    Kowalski, D.2
  • 32
    • 34250878426 scopus 로고    scopus 로고
    • Expandable DNA repeats and human disease
    • Mirkin S.M. Expandable DNA repeats and human disease. Nature 2007, 447:932-940.
    • (2007) Nature , vol.447 , pp. 932-940
    • Mirkin, S.M.1
  • 33
    • 40849134471 scopus 로고    scopus 로고
    • Role of the Saccharomyces cerevisiae Rad51 paralogs in sister chromatid recombination
    • Mozlin A.M., Fung C.W., Symington L.S. Role of the Saccharomyces cerevisiae Rad51 paralogs in sister chromatid recombination. Genetics 2008, 178:113-126.
    • (2008) Genetics , vol.178 , pp. 113-126
    • Mozlin, A.M.1    Fung, C.W.2    Symington, L.S.3
  • 34
    • 30344444484 scopus 로고    scopus 로고
    • Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
    • Murr R., Loizou J.I., Yang Y.G., Cuenin C., Li H., Wang Z.Q., Herceg Z. Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks. Nat. Cell Biol. 2006, 8:91-99.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 91-99
    • Murr, R.1    Loizou, J.I.2    Yang, Y.G.3    Cuenin, C.4    Li, H.5    Wang, Z.Q.6    Herceg, Z.7
  • 35
    • 84867302251 scopus 로고    scopus 로고
    • A role for chromatin remodellers in replication of damaged DNA
    • Niimi A., Chambers A.L., Downs J.A., Lehmann A.R. A role for chromatin remodellers in replication of damaged DNA. Nucleic Acids Res. 2012, 40:7393-7403.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 7393-7403
    • Niimi, A.1    Chambers, A.L.2    Downs, J.A.3    Lehmann, A.R.4
  • 37
    • 80053615138 scopus 로고    scopus 로고
    • RSC facilitates Rad59-dependent homologous recombination between sister chromatids by promoting cohesin loading at DNA double-strand breaks
    • Oum J.H., Seong C., Kwon Y., Ji J.H., Sid A., Ramakrishnan S., Ira G., Malkova A., Sung P., Lee S.E., Shim E.Y. RSC facilitates Rad59-dependent homologous recombination between sister chromatids by promoting cohesin loading at DNA double-strand breaks. Mol. Cell. Biol. 2011, 31:3924-3937.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3924-3937
    • Oum, J.H.1    Seong, C.2    Kwon, Y.3    Ji, J.H.4    Sid, A.5    Ramakrishnan, S.6    Ira, G.7    Malkova, A.8    Sung, P.9    Lee, S.E.10    Shim, E.Y.11
  • 39
    • 34547925170 scopus 로고    scopus 로고
    • Hat1: the emerging cellular roles of a type B histone acetyltransferase
    • Parthun M.R. Hat1: the emerging cellular roles of a type B histone acetyltransferase. Oncogene 2007, 26:5319-5328.
    • (2007) Oncogene , vol.26 , pp. 5319-5328
    • Parthun, M.R.1
  • 41
    • 39649119288 scopus 로고    scopus 로고
    • The histone acetyltransferase hMOF is frequently downregulated in primary breast carcinoma and medulloblastoma and constitutes a biomarker for clinical outcome in medulloblastoma
    • Pfister S., Rea S., Taipale M., Mendrzyk F., Straub B., Ittrich C., Thuerigen O., Sinn H.P., Akhtar A., Lichter P. The histone acetyltransferase hMOF is frequently downregulated in primary breast carcinoma and medulloblastoma and constitutes a biomarker for clinical outcome in medulloblastoma. Int. J. Cancer 2008, 122:1207-1213.
    • (2008) Int. J. Cancer , vol.122 , pp. 1207-1213
    • Pfister, S.1    Rea, S.2    Taipale, M.3    Mendrzyk, F.4    Straub, B.5    Ittrich, C.6    Thuerigen, O.7    Sinn, H.P.8    Akhtar, A.9    Lichter, P.10
  • 42
    • 0035890135 scopus 로고    scopus 로고
    • The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program
    • Pijnappel W.W., Schaft D., Roguev A., Shevchenko A., Tekotte H., Wilm M., Rigaut G., Séraphin B., Aasland R., Stewart A.F. The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program. Genes Dev. 2001, 15:2991-3004.
    • (2001) Genes Dev. , vol.15 , pp. 2991-3004
    • Pijnappel, W.W.1    Schaft, D.2    Roguev, A.3    Shevchenko, A.4    Tekotte, H.5    Wilm, M.6    Rigaut, G.7    Séraphin, B.8    Aasland, R.9    Stewart, A.F.10
  • 44
    • 84877801676 scopus 로고    scopus 로고
    • Nucleosome remodelers in double-strand break repair
    • Seeber A., Hauer M., Gasser S.M. Nucleosome remodelers in double-strand break repair. Curr. Opin. Genet. Dev. 2013, 23:174-184.
    • (2013) Curr. Opin. Genet. Dev. , vol.23 , pp. 174-184
    • Seeber, A.1    Hauer, M.2    Gasser, S.M.3
  • 47
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak M., Ishii H., Sun J.M., Pazin M.J., Davie J.R., Peterson C.L. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 2006, 311:844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 49
    • 79953753026 scopus 로고    scopus 로고
    • Expanded CAG/CTG repeat DNA induces a checkpoint response that impacts cell proliferation in Saccharomyces cerevisiae
    • Sundararajan R., Freudenreich C.H. Expanded CAG/CTG repeat DNA induces a checkpoint response that impacts cell proliferation in Saccharomyces cerevisiae. PLoS Genet. 2011, 7:e1001339.
    • (2011) PLoS Genet. , vol.7 , pp. e1001339
    • Sundararajan, R.1    Freudenreich, C.H.2
  • 50
    • 74249111370 scopus 로고    scopus 로고
    • Double-strand break repair pathways protect against CAG/CTG repeat expansions, contractions and repeat-mediated chromosomal fragility in Saccharomyces cerevisiae
    • Sundararajan R., Gellon L., Zunder R.M., Freudenreich C.H. Double-strand break repair pathways protect against CAG/CTG repeat expansions, contractions and repeat-mediated chromosomal fragility in Saccharomyces cerevisiae. Genetics 2010, 184:65-77.
    • (2010) Genetics , vol.184 , pp. 65-77
    • Sundararajan, R.1    Gellon, L.2    Zunder, R.M.3    Freudenreich, C.H.4
  • 52
    • 20344364883 scopus 로고    scopus 로고
    • Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair
    • Tamburini B.A., Tyler J.K. Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair. Mol. Cell. Biol. 2005, 25:4903-4913.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4903-4913
    • Tamburini, B.A.1    Tyler, J.K.2
  • 54
    • 78649702212 scopus 로고    scopus 로고
    • Replication and recombination factors contributing to recombination-dependent bypass of DNA lesions by template switch
    • Vanoli F., Fumasoni M., Szakal B., Maloisel L., Branzei D. Replication and recombination factors contributing to recombination-dependent bypass of DNA lesions by template switch. PLoS Genet. 2010, 6:e1001205.
    • (2010) PLoS Genet. , vol.6 , pp. e1001205
    • Vanoli, F.1    Fumasoni, M.2    Szakal, B.3    Maloisel, L.4    Branzei, D.5
  • 55
    • 34347218214 scopus 로고    scopus 로고
    • Chromatin structure of repeating CTG/CAG and CGG/CCG sequences in human disease
    • Wang Y.H. Chromatin structure of repeating CTG/CAG and CGG/CCG sequences in human disease. Front. Biosci. 2007, 12:4731-4741.
    • (2007) Front. Biosci. , vol.12 , pp. 4731-4741
    • Wang, Y.H.1
  • 57
    • 27644590452 scopus 로고    scopus 로고
    • The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination
    • Zhang H., Lawrence C.W. The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination. Proc. Natl. Acad. Sci. USA 2005, 102:15954-15959.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15954-15959
    • Zhang, H.1    Lawrence, C.W.2
  • 58
    • 79851496150 scopus 로고    scopus 로고
    • Histone H4 lysine 12 acetylation regulates telomeric heterochromatin plasticity in Saccharomyces cerevisiae
    • Zhou B.O., Wang S.S., Zhang Y., Fu X.H., Dang W., Lenzmeier B.A., Zhou J.Q. Histone H4 lysine 12 acetylation regulates telomeric heterochromatin plasticity in Saccharomyces cerevisiae. PLoS Genet. 2011, 7:e1001272.
    • (2011) PLoS Genet. , vol.7 , pp. e1001272
    • Zhou, B.O.1    Wang, S.S.2    Zhang, Y.3    Fu, X.H.4    Dang, W.5    Lenzmeier, B.A.6    Zhou, J.Q.7


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