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

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Pages 14-20 | Received 09 Nov 2015, Accepted 23 Nov 2015, Published online: 02 Mar 2016

References

  • Schulze JM, Wang AY, Kobor MS. 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
  • Le Masson I, Yu DY, Jensen K, Chevalier A, Courbeyrette R, Boulard Y, Smith MM, Mann C. 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
  • Li Y, Wen H, Xi Y, Tanaka K, Wang H, Peng D, Ren Y, Jin Q, Dent SY, Li W, et al. 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
  • Shanle EK, Andrews FH, Meriesh H, McDaniel SL, Dronamraju R, DiFiore JV, Jha D, Wozniak GG, Bridgers JB, Kerschner JL, et al. Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response. Genes Dev 2015; 29:1795-800; PMID:26341557; http://dx.doi.org/10.1101/gad.269977.115
  • Schulze JM, Wang AY, Kobor MS. 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
  • Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM. Structure and ligand of a histone acetyltransferase bromodomain. Nature 1999; 399:491-6; PMID:10365964; http://dx.doi.org/10.1038/20974
  • Lange M, Kaynak B, Forster UB, Tonjes M, Fischer JJ, Grimm C, Schlesinger J, Just S, Dunkel I, Krueger T, et al. 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
  • Zeng L, Zhang Q, Li S, Plotnikov AN, Walsh MJ, Zhou MM. 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
  • Su D, Hu Q, Li Q, Thompson JR, Cui G, Fazly A, Davies BA, Botuyan MV, Zhang Z, Mer G. 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
  • Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, et al. Histone recognition and large-scale structural analysis of the human bromodomain family. Cell 2012; 149:214-31; PMID:22464331; http://dx.doi.org/10.1016/j.cell.2012.02.013
  • Bernstein BE, Kamal M, Lindblad-Toh K, Bekiranov S, Bailey DK, Huebert DJ, McMahon S, Karlsson EK, Kulbokas EJ, 3rd, Gingeras TR, et al. Genomic maps and comparative analysis of histone modifications in human and mouse. Cell 2005; 120:169-81; PMID:15680324; http://dx.doi.org/10.1016/j.cell.2005.01.001
  • Meyer C, Hofmann J, Burmeister T, Groger D, Park TS, Emerenciano M, Pombo de Oliveira M, Renneville A, Villarese P, Macintyre E, et al. The MLL recombinome of acute leukemias in 2013. Leukemia 2013; 27:2165-76; PMID:23628958; http://dx.doi.org/10.1038/leu.2013.135
  • Collins EC, Appert A, Ariza-McNaughton L, Pannell R, Yamada Y, Rabbitts TH. 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
  • Lin C, Smith ER, Takahashi H, Lai KC, Martin-Brown S, Florens L, Washburn MP, Conaway JW, Conaway RC, Shilatifard A. 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
  • Sobhian B, Laguette N, Yatim A, Nakamura M, Levy Y, Kiernan R, Benkirane M. 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
  • Yokoyama A, Lin M, Naresh A, Kitabayashi I, Cleary ML. 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
  • He N, Chan CK, Sobhian B, Chou S, Xue Y, Liu M, Alber T, Benkirane M, Zhou Q. 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
  • Zhang W, Xia X, Reisenauer MR, Hemenway CS, Kone BC. 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
  • Luo Z, Lin C, Shilatifard A. The super elongation complex (SEC) family in transcriptional control. Nature reviews. Mol Cell Biol 2012; 13:543-7; PMID:22895430
  • Kabani M, Michot K, Boschiero C, Werner M. 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
  • Shen X. 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
  • Cairns BR, Henry NL, Kornberg RD. 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
  • John S, Howe L, Tafrov ST, Grant PA, Sternglanz R, Workman JL. 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
  • Schulze JM, Kane CM, Ruiz-Manzano A. 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
  • Zhang W, Zhang J, Zhang X, Xu C, Tu X. 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
  • Gayatri S, Bedford MT. 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
  • Blus BJ, Wiggins K, Khorasanizadeh S. Epigenetic virtues of chromodomains. Crit Rev Biochem Mol Biol 2011; 46:507-26; PMID:22023491
  • Fischle W, Tseng BS, Dormann HL, Ueberheide BM, Garcia BA, Shabanowitz J, Hunt DF, Funabiki H, Allis CD. Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature 2005; 438:1116-22; PMID:16222246; http://dx.doi.org/10.1038/nature04219
  • Hirota T, Lipp JJ, Toh BH, Peters JM. 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
  • Garske AL, Oliver SS, Wagner EK, Musselman CA, LeRoy G, Garcia BA, Kutateladze TG, Denu JM. Combinatorial profiling of chromatin binding modules reveals multisite discrimination. Nat Chem Biol 2010; 6:283-90; PMID:20190764; http://dx.doi.org/10.1038/nchembio.319
  • Varier RA, Outchkourov NS, de Graaf P, van Schaik FM, Ensing HJ, Wang F, Higgins JM, Kops GJ, Timmers HT. A phospho/methyl switch at histone H3 regulates TFIID association with mitotic chromosomes. EMBO J 2010; 29:3967-78; PMID:20953165; http://dx.doi.org/10.1038/emboj.2010.261
  • Gatchalian J, Futterer A, Rothbart SB, Tong Q, Rincon-Arano H, Sanchez de Diego A, Groudine M, Strahl BD, Martinez AC, van Wely KH, et al. Dido3 PHD modulates cell differentiation and division. Cell Rep 2013; 4:148-58; PMID:23831028; http://dx.doi.org/10.1016/j.celrep.2013.06.014
  • Ali M, Rincon-Arano H, Zhao W, Rothbart SB, Tong Q, Parkhurst SM, Strahl BD, Deng LW, Groudine M, Kutateladze TG. Molecular basis for chromatin binding and regulation of MLL5. Proc Natl Acad Sci U S A 2013; 110:11296-301; PMID:23798402; http://dx.doi.org/10.1073/pnas.1310156110
  • Voigt P, Reinberg D. 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
  • Zhao R, Nakamura T, Fu Y, Lazar Z, Spector DL. 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
  • Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S. 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

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