메뉴 건너뛰기




Volumn 4, Issue , 2014, Pages 996-1006

Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complex

Author keywords

ChIP on chip; Chromatin; Histones; Pdp3; TAP MS strategy; Yeast

Indexed keywords

FUNGAL PROTEIN; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE NUA3; HISTONE H3; HISTONE H4; SAS3P PROTEIN; TRANSCRIPTION FACTOR SAGA; UNCLASSIFIED DRUG;

EID: 84912049472     PISSN: None     EISSN: 22115463     Source Type: Journal    
DOI: 10.1016/j.fob.2014.11.001     Document Type: Article
Times cited : (14)

References (59)
  • 1
    • 79957863741 scopus 로고    scopus 로고
    • Capturing the dynamic epigenome
    • Deal R.B., Henikoff S. Capturing the dynamic epigenome. Genome Biol. 2010, 11:218.
    • (2010) Genome Biol. , vol.11 , pp. 218
    • Deal, R.B.1    Henikoff, S.2
  • 2
    • 24344466882 scopus 로고    scopus 로고
    • DNA methylation and histone modifications: teaming up to silence genes
    • Fuks F. DNA methylation and histone modifications: teaming up to silence genes. Curr. Opin. Genet. Dev. 2005, 15:490-495.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 490-495
    • Fuks, F.1
  • 3
    • 34250192537 scopus 로고    scopus 로고
    • Mechanisms of epigenetic inheritance
    • Martin C., Zhang Y. Mechanisms of epigenetic inheritance. Curr. Opin. Cell Biol. 2007, 19:266-272.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 266-272
    • Martin, C.1    Zhang, Y.2
  • 4
    • 84863986133 scopus 로고    scopus 로고
    • Functions of DNA methylation: islands, start sites, gene bodies and beyond
    • Jones P.A. Functions of DNA methylation: islands, start sites, gene bodies and beyond. Nat. Rev. Genet. 2012, 13:484-492.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 484-492
    • Jones, P.A.1
  • 5
    • 80052805267 scopus 로고    scopus 로고
    • Histone modification: cause or cog?
    • Henikoff S., Shilatifard A. Histone modification: cause or cog?. Trends Genet. 2011, 27:389-396.
    • (2011) Trends Genet. , vol.27 , pp. 389-396
    • Henikoff, S.1    Shilatifard, A.2
  • 6
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature 2000, 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 7
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science 2001, 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 8
    • 0027366656 scopus 로고
    • The role of histones and their modifications in the informative content of chromatin
    • Tordera V., Sendra R., Perez-Ortin J.E. The role of histones and their modifications in the informative content of chromatin. Experientia 1993, 49:780-788.
    • (1993) Experientia , vol.49 , pp. 780-788
    • Tordera, V.1    Sendra, R.2    Perez-Ortin, J.E.3
  • 9
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner B.M. Decoding the nucleosome. Cell 1993, 75:5-8.
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 10
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister A.J., Kouzarides T. Regulation of chromatin by histone modifications. Cell Res. 2011, 21:381-395.
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 11
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: one size doesn't fit all
    • Lee K.K., Workman J.L. Histone acetyltransferase complexes: one size doesn't fit all. Nat. Rev. Mol. Cell Biol. 2007, 8:284-295.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 12
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • Shahbazian M.D., Grunstein M. Functions of site-specific histone acetylation and deacetylation. Annu. Rev. Biochem. 2007, 76:75-100.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 13
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger S.L. The complex language of chromatin regulation during transcription. Nature 2007, 447:407-412.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 14
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007, 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 15
    • 34547916813 scopus 로고    scopus 로고
    • Moving marks: dynamic histone modifications in yeast
    • Krebs J.E. Moving marks: dynamic histone modifications in yeast. Mol. BioSyst. 2007, 3:590-597.
    • (2007) Mol. BioSyst. , vol.3 , pp. 590-597
    • Krebs, J.E.1
  • 16
    • 0035957097 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in Saccharomyces cerevisiae
    • Waterborg J.H. Dynamics of histone acetylation in Saccharomyces cerevisiae. Biochemistry 2001, 40:2599-2605.
    • (2001) Biochemistry , vol.40 , pp. 2599-2605
    • Waterborg, J.H.1
  • 18
    • 33645224956 scopus 로고    scopus 로고
    • Genome-wide relationships between TAF1 and histone acetyltransferases in Saccharomyces cerevisiae
    • Durant M., Pugh B.F. Genome-wide relationships between TAF1 and histone acetyltransferases in Saccharomyces cerevisiae. Mol. Cell. Biol. 2006, 26:2791-2802.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2791-2802
    • Durant, M.1    Pugh, B.F.2
  • 19
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • Howe L., Auston D., Grant P., John S., Cook R.G., Workman J.L., Pillus L. Histone H3 specific acetyltransferases are essential for cell cycle progression. Genes Dev. 2001, 15:3144-3154.
    • (2001) Genes Dev. , vol.15 , pp. 3144-3154
    • Howe, L.1    Auston, D.2    Grant, P.3    John, S.4    Cook, R.G.5    Workman, J.L.6    Pillus, L.7
  • 22
    • 76849084692 scopus 로고    scopus 로고
    • A role for Gcn5 in replication-coupled nucleosome assembly
    • Burgess R.J., Zhou H., Han J., Zhang Z. A role for Gcn5 in replication-coupled nucleosome assembly. Mol. Cell 2010, 37:469-480.
    • (2010) Mol. Cell , vol.37 , pp. 469-480
    • Burgess, R.J.1    Zhou, H.2    Han, J.3    Zhang, Z.4
  • 23
    • 0034657420 scopus 로고    scopus 로고
    • The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex
    • John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L. The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex. Genes Dev. 2000, 14:1196-1208.
    • (2000) Genes Dev. , vol.14 , pp. 1196-1208
    • John, S.1    Howe, L.2    Tafrov, S.T.3    Grant, P.A.4    Sternglanz, R.5    Workman, J.L.6
  • 24
    • 33645804789 scopus 로고    scopus 로고
    • Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatin
    • Martin D.G.E., Grimes D.E., Baetz K., Howe L. Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatin. Mol. Cell. Biol. 2006, 26:3018-3028.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3018-3028
    • Martin, D.G.E.1    Grimes, D.E.2    Baetz, K.3    Howe, L.4
  • 26
    • 33845968873 scopus 로고    scopus 로고
    • Gcn5 promotes acetylation, eviction, and methylation of nucleosomes in transcribed coding regions
    • Govind C.K., Zhang F., Qiu H., Hofmeyer K., Hinnebusch A.G. Gcn5 promotes acetylation, eviction, and methylation of nucleosomes in transcribed coding regions. Mol. Cell 2007, 25:31-42.
    • (2007) Mol. Cell , vol.25 , pp. 31-42
    • Govind, C.K.1    Zhang, F.2    Qiu, H.3    Hofmeyer, K.4    Hinnebusch, A.G.5
  • 28
    • 34347348213 scopus 로고    scopus 로고
    • Selective requirement for SAGA in Hog1-mediated gene expression depending on the severity of the external osmostress conditions
    • Zapater M., Sohrmann M., Peter M., Posas F., De Nadal E. Selective requirement for SAGA in Hog1-mediated gene expression depending on the severity of the external osmostress conditions. Mol. Cell. Biol. 2007, 27:3900-3910.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3900-3910
    • Zapater, M.1    Sohrmann, M.2    Peter, M.3    Posas, F.4    De Nadal, E.5
  • 29
    • 33751527233 scopus 로고    scopus 로고
    • Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
    • Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H., Baker L., Boyle J., Blair L.P., Chait B., et al. Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol. Cell 2006, 24:785-796.
    • (2006) Mol. Cell , vol.24 , pp. 785-796
    • Taverna, S.D.1    Ilin, S.2    Rogers, R.S.3    Tanny, J.C.4    Lavender, H.5    Li, H.6    Baker, L.7    Boyle, J.8    Blair, L.P.9    Chait, B.10
  • 30
    • 57349156720 scopus 로고    scopus 로고
    • Acetylation of Rsc4p by Gcn5p is essential in the absence of histone H3 acetylation
    • Choi J.K., Grimes D.E., Rowe K.M., Howe L.J. Acetylation of Rsc4p by Gcn5p is essential in the absence of histone H3 acetylation. Mol. Cell. Biol. 2008, 28:6967-6972.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6967-6972
    • Choi, J.K.1    Grimes, D.E.2    Rowe, K.M.3    Howe, L.J.4
  • 31
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • Zhang W., Bone J.R., Edmondson D.G., Turner B.M., Roth S.Y. Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase. EMBO J. 1998, 17:3155-3167.
    • (1998) EMBO J. , vol.17 , pp. 3155-3167
    • Zhang, W.1    Bone, J.R.2    Edmondson, D.G.3    Turner, B.M.4    Roth, S.Y.5
  • 32
    • 84868116575 scopus 로고    scopus 로고
    • Functional antagonism between Sas3 and Gcn5 acetyltransferases and ISWI chromatin remodelers
    • Lafon A., Petty E., Pillus L. Functional antagonism between Sas3 and Gcn5 acetyltransferases and ISWI chromatin remodelers. PLoS Genet. 2012, 8:e1002994.
    • (2012) PLoS Genet. , vol.8 , pp. e1002994
    • Lafon, A.1    Petty, E.2    Pillus, L.3
  • 33
    • 84901344915 scopus 로고    scopus 로고
    • Unexpected function of the glucanosyltransferase Gas1 in the DNA damage response linked to histone H3 acetyltransferases in Saccharomyces cerevisiae
    • Eustice M., Pillus L. Unexpected function of the glucanosyltransferase Gas1 in the DNA damage response linked to histone H3 acetyltransferases in Saccharomyces cerevisiae. Genetics 2014, 196:1029-1039.
    • (2014) Genetics , vol.196 , pp. 1029-1039
    • Eustice, M.1    Pillus, L.2
  • 34
    • 34547861703 scopus 로고    scopus 로고
    • MYST opportunities for growth control: yeast genes illuminate human cancer gene functions
    • Lafon A., Chang C.S., Scott E.M., Jacobson S.J., Pillus L. MYST opportunities for growth control: yeast genes illuminate human cancer gene functions. Oncogene 2007, 26:5373-5384.
    • (2007) Oncogene , vol.26 , pp. 5373-5384
    • Lafon, A.1    Chang, C.S.2    Scott, E.M.3    Jacobson, S.J.4    Pillus, L.5
  • 35
    • 84874344108 scopus 로고    scopus 로고
    • Quantitating the specificity and selectivity of Gcn5-mediated acetylation of histone H3
    • Kuo Y.M., Andrews A.J. Quantitating the specificity and selectivity of Gcn5-mediated acetylation of histone H3. PLoS ONE 2013, 8:e54896.
    • (2013) PLoS ONE , vol.8 , pp. e54896
    • Kuo, Y.M.1    Andrews, A.J.2
  • 41
    • 84910679960 scopus 로고    scopus 로고
    • An H3K36me3 binding PWWP protein targets the NuA3 acetyltransferase complex to coordinate transcriptional elongation at coding regions
    • mcp.M114.038224
    • Gilbert T.M., McDaniel S.L., Byrum S.D., Cades J.A., Dancy B.C., Wade H., Tackett A.J., Strahl B.D., Taverna S.D. An H3K36me3 binding PWWP protein targets the NuA3 acetyltransferase complex to coordinate transcriptional elongation at coding regions. Mol. Cell. Proteomics 2014, 13:2883-2895. mcp.M114.038224.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2883-2895
    • Gilbert, T.M.1    McDaniel, S.L.2    Byrum, S.D.3    Cades, J.A.4    Dancy, B.C.5    Wade, H.6    Tackett, A.J.7    Strahl, B.D.8    Taverna, S.D.9
  • 43
  • 44
    • 84868617799 scopus 로고    scopus 로고
    • The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation
    • Dastidar R., Hooda J., Shah A., Cao T., Henke R., Zhang L. The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation. Cell Biosci. 2012, 2:30.
    • (2012) Cell Biosci. , vol.2 , pp. 30
    • Dastidar, R.1    Hooda, J.2    Shah, A.3    Cao, T.4    Henke, R.5    Zhang, L.6
  • 45
    • 84897450989 scopus 로고    scopus 로고
    • Dynamic remodeling of histone modifications in response to osmotic stress in Saccharomyces cerevisiae
    • Magraner-Pardo L., Pelechano V., Coloma M.D., Tordera V. Dynamic remodeling of histone modifications in response to osmotic stress in Saccharomyces cerevisiae. BMC Genomics 2014, 15:247. 10.1186/1471-2164-15-247.
    • (2014) BMC Genomics , vol.15 , pp. 247
    • Magraner-Pardo, L.1    Pelechano, V.2    Coloma, M.D.3    Tordera, V.4
  • 48
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Seraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 1999, 17:1030-1032.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 50
    • 54249139981 scopus 로고    scopus 로고
    • An easy assay for histone acetyltransferase activity using a phosphorimager
    • Poveda A., Sendra R. An easy assay for histone acetyltransferase activity using a phosphorimager. Anal. Biochem. 2008, 383:296-300.
    • (2008) Anal. Biochem. , vol.383 , pp. 296-300
    • Poveda, A.1    Sendra, R.2
  • 51
    • 0031056461 scopus 로고    scopus 로고
    • Gcn5p is involved in the acetylation of histone H3 in nucleosomes
    • Ruiz-García A.B., Sendra R., Pamblanco M., Tordera V. Gcn5p is involved in the acetylation of histone H3 in nucleosomes. FEBS Lett. 1997, 403:186-190.
    • (1997) FEBS Lett. , vol.403 , pp. 186-190
    • Ruiz-García, A.B.1    Sendra, R.2    Pamblanco, M.3    Tordera, V.4
  • 52
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov V.V. Rapid and reliable protein extraction from yeast. Yeast 2000, 16:857-860.
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 53
    • 0028951895 scopus 로고
    • Rapid and effective Western blotting of histones from acid-urea-triton and sodium dodecyl sulfate polyacrylamide gels: two different approaches depending on the subsequent qualitative or quantitative analysis
    • Thiriet C., Albert P. Rapid and effective Western blotting of histones from acid-urea-triton and sodium dodecyl sulfate polyacrylamide gels: two different approaches depending on the subsequent qualitative or quantitative analysis. Electrophoresis 1995, 16:357-361.
    • (1995) Electrophoresis , vol.16 , pp. 357-361
    • Thiriet, C.1    Albert, P.2
  • 55
    • 67349226123 scopus 로고    scopus 로고
    • Identification of immunoreactive proteins from the dog heartworm (Dirofilaria immitis) differentially recognized by the sera from dogs with patent or occult infections
    • Oleaga A., Pérez-Sánchez R., Pagés E., Marcos-Atxutegi C., Simón F. Identification of immunoreactive proteins from the dog heartworm (Dirofilaria immitis) differentially recognized by the sera from dogs with patent or occult infections. Mol. Biochem. Parasitol. 2009, 166:134-141.
    • (2009) Mol. Biochem. Parasitol. , vol.166 , pp. 134-141
    • Oleaga, A.1    Pérez-Sánchez, R.2    Pagés, E.3    Marcos-Atxutegi, C.4    Simón, F.5
  • 57
    • 0030971236 scopus 로고    scopus 로고
    • Construction of a yeast strain deleted for the TRP1 promoter and coding region that enhances the efficiency of the polymerase chain reaction-disruption method
    • Baudin-Baillieu A., Guillemet E., Cullin C., Lacroute F. Construction of a yeast strain deleted for the TRP1 promoter and coding region that enhances the efficiency of the polymerase chain reaction-disruption method. Yeast 1997, 13:353-356.
    • (1997) Yeast , vol.13 , pp. 353-356
    • Baudin-Baillieu, A.1    Guillemet, E.2    Cullin, C.3    Lacroute, F.4
  • 58
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R.S., Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 1989, 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 59
    • 42449087717 scopus 로고    scopus 로고
    • Site specificity of yeast histone acetyltransferase B complex in vivo
    • Poveda A., Sendra R. Site specificity of yeast histone acetyltransferase B complex in vivo. FEBS J. 2008, 275:2122-2136.
    • (2008) FEBS J. , vol.275 , pp. 2122-2136
    • Poveda, A.1    Sendra, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.