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Volumn 7, Issue 1, 2016, Pages 14-20

The essential role of acetyllysine binding by the YEATS domain in transcriptional regulation

Author keywords

acetyllysine; AF9; Taf14; transcription; YEATS domain

Indexed keywords

ACETIC ACID DERIVATIVE; ACETYLLYSINE; RNA POLYMERASE II; UNCLASSIFIED DRUG; DOT1L PROTEIN, HUMAN; LYSINE; METHYLTRANSFERASE; MLLT3 PROTEIN, HUMAN; NUCLEAR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TAF14 PROTEIN, S CEREVISIAE; TRANSCRIPTION FACTOR IID;

EID: 84960376013     PISSN: 21541264     EISSN: 21541272     Source Type: Journal    
DOI: 10.1080/21541264.2015.1125987     Document Type: Review
Times cited : (26)

References (36)
  • 1
    • 78449239049 scopus 로고    scopus 로고
    • Reading chromatin: insights from yeast into YEATS domain structure and function
    • 20657183
    • J.M.Schulze, A.Y.Wang, M.S.Kobor. Reading chromatin: insights from yeast into YEATS domain structure and function. Epigenetics 2010; 5:573-7; PMID:20657183; http://dx.doi.org/10.4161/epi.5.7.12856
    • (2010) Epigenetics , vol.5 , pp. 573-577
    • Schulze, J.M.1    Wang, A.Y.2    Kobor, M.S.3
  • 2
    • 0042470632 scopus 로고    scopus 로고
    • Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the cellular response to spindle stress in yeast
    • 12917332
    • I.Le Masson, D.Y.Yu, K.Jensen, A.Chevalier, R.Courbeyrette, Y.Boulard, M.M.Smith, C.Mann. Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the cellular response to spindle stress in yeast. Mol Cell Biol 2003; 23:6086-102; PMID:12917332; http://dx.doi.org/10.1128/MCB.23.17.6086-6102.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 6086-6102
    • Le Masson, I.1    Yu, D.Y.2    Jensen, K.3    Chevalier, A.4    Courbeyrette, R.5    Boulard, Y.6    Smith, M.M.7    Mann, C.8
  • 3
    • 84908273616 scopus 로고    scopus 로고
    • AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation
    • 25417107
    • Y.Li, H.Wen, Y.Xi, K.Tanaka, H.Wang, D.Peng, Y.Ren, Q.Jin, S.Y.Dent, W.Li, AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation. Cell 2014; 159:558-71; PMID:25417107; http://dx.doi.org/10.1016/j.cell.2014.09.049
    • (2014) Cell , vol.159 , pp. 558-571
    • Li, Y.1    Wen, H.2    Xi, Y.3    Tanaka, K.4    Wang, H.5    Peng, D.6    Ren, Y.7    Jin, Q.8    Dent, S.Y.9    Li, W.10
  • 5
    • 65249180695 scopus 로고    scopus 로고
    • YEATS domain proteins: a diverse family with many links to chromatin modification and transcription
    • 19234524
    • J.M.Schulze, A.Y.Wang, M.S.Kobor. YEATS domain proteins: a diverse family with many links to chromatin modification and transcription. Biochem Cell Biol 2009; 87:65-75; PMID:19234524; http://dx.doi.org/10.1139/O08-111
    • (2009) Biochem Cell Biol , vol.87 , pp. 65-75
    • Schulze, J.M.1    Wang, A.Y.2    Kobor, M.S.3
  • 6
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • 10365964
    • C.Dhalluin, J.E.Carlson, L.Zeng, C.He, A.K.Aggarwal, M.M.Zhou. Structure and ligand of a histone acetyltransferase bromodomain. Nature 1999; 399:491-6; PMID:10365964; http://dx.doi.org/10.1038/20974
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.M.6
  • 7
    • 51149107006 scopus 로고    scopus 로고
    • Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex
    • 18765789
    • M.Lange, B.Kaynak, U.B.Forster, M.Tonjes, J.J.Fischer, C.Grimm, J.Schlesinger, S.Just, I.Dunkel, T.Krueger, Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex. Genes Dev 2008; 22:2370-84; PMID:18765789; http://dx.doi.org/10.1101/gad.471408
    • (2008) Genes Dev , vol.22 , pp. 2370-2384
    • Lange, M.1    Kaynak, B.2    Forster, U.B.3    Tonjes, M.4    Fischer, J.J.5    Grimm, C.6    Schlesinger, J.7    Just, S.8    Dunkel, I.9    Krueger, T.10
  • 8
    • 77954487796 scopus 로고    scopus 로고
    • Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b
    • 20613843
    • L.Zeng, Q.Zhang, S.Li, A.N.Plotnikov, M.J.Walsh, M.M.Zhou. Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b. Nature 2010; 466:258-62; PMID:20613843; http://dx.doi.org/10.1038/nature09139
    • (2010) Nature , vol.466 , pp. 258-262
    • Zeng, L.1    Zhang, Q.2    Li, S.3    Plotnikov, A.N.4    Walsh, M.J.5    Zhou, M.M.6
  • 9
    • 84862776630 scopus 로고    scopus 로고
    • Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106
    • 22307274
    • D.Su, Q.Hu, Q.Li, J.R.Thompson, G.Cui, A.Fazly, B.A.Davies, M.V.Botuyan, Z.Zhang, G.Mer. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature 2012; 483:104-7; PMID:22307274; http://dx.doi.org/10.1038/nature10861
    • (2012) Nature , vol.483 , pp. 104-107
    • Su, D.1    Hu, Q.2    Li, Q.3    Thompson, J.R.4    Cui, G.5    Fazly, A.6    Davies, B.A.7    Botuyan, M.V.8    Zhang, Z.9    Mer, G.10
  • 13
    • 0036788729 scopus 로고    scopus 로고
    • Mouse Af9 is a controller of embryo patterning, like Mll, whose human homologue fuses with Af9 after chromosomal translocation in leukemia
    • 12242306
    • E.C.Collins, A.Appert, L.Ariza-McNaughton, R.Pannell, Y.Yamada, T.H.Rabbitts. Mouse Af9 is a controller of embryo patterning, like Mll, whose human homologue fuses with Af9 after chromosomal translocation in leukemia. Mol Cell Biol 2002; 22:7313-24; PMID:12242306; http://dx.doi.org/10.1128/MCB.22.20.7313-7324.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 7313-7324
    • Collins, E.C.1    Appert, A.2    Ariza-McNaughton, L.3    Pannell, R.4    Yamada, Y.5    Rabbitts, T.H.6
  • 14
    • 75949126139 scopus 로고    scopus 로고
    • AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia
    • 20159561
    • C.Lin, E.R.Smith, H.Takahashi, K.C.Lai, S.Martin-Brown, L.Florens, M.P.Washburn, J.W.Conaway, R.C.Conaway, A.Shilatifard. AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia. Mol Cell 2010; 37:429-37; PMID:20159561; http://dx.doi.org/10.1016/j.molcel.2010.01.026
    • (2010) Mol Cell , vol.37 , pp. 429-437
    • Lin, C.1    Smith, E.R.2    Takahashi, H.3    Lai, K.C.4    Martin-Brown, S.5    Florens, L.6    Washburn, M.P.7    Conaway, J.W.8    Conaway, R.C.9    Shilatifard, A.10
  • 15
    • 77951954237 scopus 로고    scopus 로고
    • HIV-1 Tat assembles a multifunctional transcription elongation complex and stably associates with the 7SK snRNP
    • 20471949
    • B.Sobhian, N.Laguette, A.Yatim, M.Nakamura, Y.Levy, R.Kiernan, M.Benkirane. HIV-1 Tat assembles a multifunctional transcription elongation complex and stably associates with the 7SK snRNP. Mol Cell 2010; 38:439-51; PMID:20471949; http://dx.doi.org/10.1016/j.molcel.2010.04.012
    • (2010) Mol Cell , vol.38 , pp. 439-451
    • Sobhian, B.1    Laguette, N.2    Yatim, A.3    Nakamura, M.4    Levy, Y.5    Kiernan, R.6    Benkirane, M.7
  • 16
    • 76349118080 scopus 로고    scopus 로고
    • A higher-order complex containing AF4 and ENL family proteins with P-TEFb facilitates oncogenic and physiologic MLL-dependent transcription
    • 20153263
    • A.Yokoyama, M.Lin, A.Naresh, I.Kitabayashi, M.L.Cleary. A higher-order complex containing AF4 and ENL family proteins with P-TEFb facilitates oncogenic and physiologic MLL-dependent transcription. Cancer Cell 2010; 17:198-212; PMID:20153263; http://dx.doi.org/10.1016/j.ccr.2009.12.040
    • (2010) Cancer Cell , vol.17 , pp. 198-212
    • Yokoyama, A.1    Lin, M.2    Naresh, A.3    Kitabayashi, I.4    Cleary, M.L.5
  • 17
    • 80052571366 scopus 로고    scopus 로고
    • Human Polymerase-Associated Factor complex (PAFc) connects the Super Elongation Complex (SEC) to RNA polymerase II on chromatin
    • 21873227
    • N.He, C.K.Chan, B.Sobhian, S.Chou, Y.Xue, M.Liu, T.Alber, M.Benkirane, Q.Zhou. Human Polymerase-Associated Factor complex (PAFc) connects the Super Elongation Complex (SEC) to RNA polymerase II on chromatin. Proc Natl Acad Sci U S A 2011; 108:E636-45; PMID:21873227; http://dx.doi.org/10.1073/pnas.1107107108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. E636-E645
    • He, N.1    Chan, C.K.2    Sobhian, B.3    Chou, S.4    Xue, Y.5    Liu, M.6    Alber, T.7    Benkirane, M.8    Zhou, Q.9
  • 18
    • 33745873838 scopus 로고    scopus 로고
    • Dot1a-AF9 complex mediates histone H3 Lys-79 hypermethylation and repression of ENaCalpha in an aldosterone-sensitive manner
    • 16636056
    • W.Zhang, X.Xia, M.R.Reisenauer, C.S.Hemenway, B.C.Kone. Dot1a-AF9 complex mediates histone H3 Lys-79 hypermethylation and repression of ENaCalpha in an aldosterone-sensitive manner. J Biol Chem 2006; 281:18059-68; PMID:16636056; http://dx.doi.org/10.1074/jbc.M601903200
    • (2006) J Biol Chem , vol.281 , pp. 18059-18068
    • Zhang, W.1    Xia, X.2    Reisenauer, M.R.3    Hemenway, C.S.4    Kone, B.C.5
  • 19
    • 84865419994 scopus 로고    scopus 로고
    • The super elongation complex (SEC) family in transcriptional control. Nature reviews
    • 22895430
    • Z.Luo, C.Lin, A.Shilatifard. The super elongation complex (SEC) family in transcriptional control. Nature reviews. Mol Cell Biol 2012; 13:543-7; PMID:22895430
    • (2012) Mol Cell Biol , vol.13 , pp. 543-547
    • Luo, Z.1    Lin, C.2    Shilatifard, A.3
  • 20
    • 19444366248 scopus 로고    scopus 로고
    • Anc1 interacts with the catalytic subunits of the general transcription factors TFIID and TFIIF, the chromatin remodeling complexes RSC and INO80, and the histone acetyltransferase complex NuA3
    • 15896708
    • M.Kabani, K.Michot, C.Boschiero, M.Werner. Anc1 interacts with the catalytic subunits of the general transcription factors TFIID and TFIIF, the chromatin remodeling complexes RSC and INO80, and the histone acetyltransferase complex NuA3. Biochem Biophys Res Commun 2005; 332:398-403; PMID:15896708; http://dx.doi.org/10.1016/j.bbrc.2005.04.158
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 398-403
    • Kabani, M.1    Michot, K.2    Boschiero, C.3    Werner, M.4
  • 21
    • 0842282836 scopus 로고    scopus 로고
    • Preparation and analysis of the INO80 complex
    • 14979041
    • X.Shen. Preparation and analysis of the INO80 complex. Methods Enzymol 2004; 377:401-12; PMID:14979041; http://dx.doi.org/10.1016/S0076-6879(03)77026-8
    • (2004) Methods Enzymol , vol.377 , pp. 401-412
    • Shen, X.1
  • 22
    • 0029665594 scopus 로고    scopus 로고
    • TFG/TAF30/ANC1, a component of the yeast SWI/SNF complex that is similar to the leukemogenic proteins ENL and AF-9
    • 8668146
    • B.R.Cairns, N.L.Henry, R.D.Kornberg. TFG/TAF30/ANC1, a component of the yeast SWI/SNF complex that is similar to the leukemogenic proteins ENL and AF-9. Mol Cell Biol 1996; 16:3308-16; PMID:8668146; http://dx.doi.org/10.1128/MCB.16.7.3308
    • (1996) Mol Cell Biol , vol.16 , pp. 3308-3316
    • Cairns, B.R.1    Henry, N.L.2    Kornberg, R.D.3
  • 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
    • 10817755
    • S.John, L.Howe, S.T.Tafrov, P.A.Grant, R.Sternglanz, J.L.Workman. 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; 14:1196-208; PMID:10817755
    • (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
    • 77949906545 scopus 로고    scopus 로고
    • The YEATS domain of Taf14 in Saccharomyces cerevisiae has a negative impact on cell growth
    • 20179968
    • J.M.Schulze, C.M.Kane, A.Ruiz-Manzano. The YEATS domain of Taf14 in Saccharomyces cerevisiae has a negative impact on cell growth. Mol Genet Genomics 2010; 283:365-80; PMID:20179968; http://dx.doi.org/10.1007/s00438-010-0523-x
    • (2010) Mol Genet Genomics , vol.283 , pp. 365-380
    • Schulze, J.M.1    Kane, C.M.2    Ruiz-Manzano, A.3
  • 25
    • 79955542044 scopus 로고    scopus 로고
    • Solution structure of the Taf14 YEATS domain and its roles in cell growth of Saccharomyces cerevisiae
    • 21355849
    • W.Zhang, J.Zhang, X.Zhang, C.Xu, X.Tu. Solution structure of the Taf14 YEATS domain and its roles in cell growth of Saccharomyces cerevisiae. Biochem J 2011; 436:83-90; PMID:21355849; http://dx.doi.org/10.1042/BJ20110004
    • (2011) Biochem J , vol.436 , pp. 83-90
    • Zhang, W.1    Zhang, J.2    Zhang, X.3    Xu, C.4    Tu, X.5
  • 26
    • 84904048466 scopus 로고    scopus 로고
    • Readers of histone methylarginine marks
    • 24583552
    • S.Gayatri, M.T.Bedford. Readers of histone methylarginine marks. Biochim Biophys Acta 2014; 1839:702-10; PMID:24583552; http://dx.doi.org/10.1016/j.bbagrm.2014.02.015
    • (2014) Biochim Biophys Acta , vol.1839 , pp. 702-710
    • Gayatri, S.1    Bedford, M.T.2
  • 29
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • 16222244
    • T.Hirota, J.J.Lipp, B.H.Toh, J.M.Peters. Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 2005; 438:1176-80; PMID:16222244; http://dx.doi.org/10.1038/nature04254
    • (2005) Nature , vol.438 , pp. 1176-1180
    • Hirota, T.1    Lipp, J.J.2    Toh, B.H.3    Peters, J.M.4
  • 34
    • 82255175234 scopus 로고    scopus 로고
    • BRD4 jump-starts transcription after mitotic silencing
    • 22126464
    • P.Voigt, D.Reinberg. BRD4 jump-starts transcription after mitotic silencing. Genome Biol 2011; 12:133; PMID:22126464; http://dx.doi.org/10.1186/gb-2011-12-11-133
    • (2011) Genome Biol , vol.12 , pp. 133
    • Voigt, P.1    Reinberg, D.2
  • 35
    • 80455122751 scopus 로고    scopus 로고
    • Gene bookmarking accelerates the kinetics of post-mitotic transcriptional re-activation
    • 21983563
    • R.Zhao, T.Nakamura, Y.Fu, Z.Lazar, D.L.Spector. Gene bookmarking accelerates the kinetics of post-mitotic transcriptional re-activation. Nat Cell Biol 2011; 13:1295-304; PMID:21983563; http://dx.doi.org/10.1038/ncb2341
    • (2011) Nat Cell Biol , vol.13 , pp. 1295-1304
    • Zhao, R.1    Nakamura, T.2    Fu, Y.3    Lazar, Z.4    Spector, D.L.5
  • 36
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • 15485929
    • S.Pal, S.N.Vishwanath, H.Erdjument-Bromage, P.Tempst, S.Sif. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol 2004; 24:9630-45; PMID:15485929; http://dx.doi.org/10.1128/MCB.24.21.9630-9645.2004
    • (2004) Mol Cell Biol , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5


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