Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states (original) (raw)
Bhaumik, S.R., Smith, E. & Shilatifard, A. Covalent modifications of histones during development and disease pathogenesis. Nat. Struct. Mol. Biol.14, 1008–1016 (2007). ArticleCASPubMed Google Scholar
Li, B., Carey, M. & Workman, J.L. The role of chromatin during transcription. Cell128, 707–719 (2007). ArticleCASPubMed Google Scholar
Cheng, X., Collins, R.E. & Zhang, X. Structural and sequence motifs of protein (histone) methylation enzymes. Annu. Rev. Biophys. Biomol. Struct.34, 267–294 (2005). ArticleCASPubMedPubMed Central Google Scholar
Klose, R.J. & Zhang, Y. Regulation of histone methylation by demethylimination and demethylation. Nat. Rev. Mol. Cell Biol.8, 307–318 (2007). ArticleCASPubMed Google Scholar
Shi, Y. & Whetstine, J.R. Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell25, 1–14 (2007). ArticleCASPubMed Google Scholar
Taverna, S.D., Li, H., Ruthenburg, A.J., Allis, C.D. & Patel, D.J. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nat. Struct. Mol. Biol.14, 1025–1040 (2007). ArticleCASPubMedPubMed Central Google Scholar
Sawada, K. et al. Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase. J. Biol. Chem.279, 43296–43306 (2004). ArticleCASPubMed Google Scholar
Min, J., Feng, Q., Li, Z., Zhang, Y. & Xu, R.M. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell112, 711–723 (2003). ArticleCASPubMed Google Scholar
van Leeuwen, F., Gafken, P.R. & Gottschling, D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell109, 745–756 (2002). ArticleCASPubMed Google Scholar
Okada, Y. et al. hDOT1L links histone methylation to leukemogenesis. Cell121, 167–178 (2005). ArticleCASPubMed Google Scholar
Gazin, C., Wajapeyee, N., Gobeil, S., Virbasius, C.M. & Green, M.R. An elaborate pathway required for Ras-mediated epigenetic silencing. Nature449, 1073–1077 (2007). ArticleCASPubMedPubMed Central Google Scholar
Zhang, W., Xia, X., Reisenauer, M.R., Hemenway, C.S. & Kone, B.C. Dot1a-AF9 complex mediates histone H3 Lys-79 hypermethylation and repression of ENaCα in an aldosterone-sensitive manner. J. Biol. Chem.281, 18059–18068 (2006). ArticleCASPubMed Google Scholar
Ng, H.H. et al. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev.16, 1518–1527 (2002). ArticleCASPubMedPubMed Central Google Scholar
Lacoste, N., Utley, R.T., Hunter, J.M., Poirier, G.G. & Cote, J. Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase. J. Biol. Chem.277, 30421–30424 (2002). ArticleCASPubMed Google Scholar
San Segundo, P.A. & Roeder, G.S. Role for the silencing protein Dot1 in meiotic checkpoint control. Mol. Biol. Cell11, 3601–3615 (2000). ArticleCASPubMedPubMed Central Google Scholar
Ng, H.H., Ciccone, D.N., Morshead, K.B., Oettinger, M.A. & Struhl, K. Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation. Proc. Natl. Acad. Sci. USA100, 1820–1825 (2003). ArticleCASPubMedPubMed Central Google Scholar
Giannattasio, M., Lazzaro, F., Plevani, P. & Muzi-Falconi, M. The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1. J. Biol. Chem.280, 9879–9886 (2005). ArticleCASPubMed Google Scholar
Wysocki, R. et al. 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). ArticleCASPubMedPubMed Central Google Scholar
Shahbazian, M.D., Zhang, K. & Grunstein, M. Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1. Mol. Cell19, 271–277 (2005). ArticleCASPubMed Google Scholar
Katan-Khaykovich, Y. & Struhl, K. Heterochromatin formation involves changes in histone modifications over multiple cell generations. EMBO J.24, 2138–2149 (2005). ArticleCASPubMedPubMed Central Google Scholar
Liang, G., Klose, R.J., Gardner, K.E. & Zhang, Y. Yeast Jhd2p is a histone H3 Lys4 trimethyl demethylase. Nat. Struct. Mol. Biol.14, 243–245 (2007). ArticleCASPubMed Google Scholar
Tu, S. et al. Identification of histone demethylases in Saccharomyces cerevisiae. J. Biol. Chem.282, 14262–14271 (2007). ArticleCASPubMed Google Scholar
Botuyan, M.V. et al. Structural basis for the methylation state-specific recognition of histone H4–K20 by 53BP1 and Crb2 in DNA repair. Cell127, 1361–1373 (2006). ArticleCASPubMedPubMed Central Google Scholar
Ng, H.H., Xu, R.M., Zhang, Y. & Struhl, K. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J. Biol. Chem.277, 34655–34657 (2002). ArticleCASPubMed Google Scholar
Briggs, S.D. et al. Gene silencing: _trans_-histone regulatory pathway in chromatin. Nature418, 498 (2002). ArticleCASPubMed Google Scholar
Krogan, N.J. et al. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol. Cell11, 721–729 (2003). ArticleCASPubMed Google Scholar
Zhu, B. et al. Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Mol. Cell20, 601–611 (2005). ArticleCASPubMed Google Scholar
Wang, H. et al. mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol. Cell12, 475–487 (2003). ArticleCASPubMed Google Scholar
Schneider, J. et al. Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression. Mol. Cell19, 849–856 (2005). ArticleCASPubMed Google Scholar
Dehe, P.M. et al. Protein interactions within the Set1 complex and their roles in the regulation of histone 3 lysine 4 methylation. J. Biol. Chem.281, 35404–35412 (2006). ArticleCASPubMed Google Scholar
Dou, Y. et al. Regulation of MLL1 H3K4 methyltransferase activity by its core components. Nat. Struct. Mol. Biol.13, 713–719 (2006). ArticleCASPubMed Google Scholar
Fingerman, I.M., Li, H.C. & Briggs, S.D. A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new _trans_-histone pathway. Genes Dev.21, 2018–2029 (2007). ArticleCASPubMedPubMed Central Google Scholar
Schwabish, M.A. & Struhl, K. Evidence for eviction and rapid deposition of histones upon transcriptional elongation by RNA polymerase II. Mol. Cell. Biol.24, 10111–10117 (2004). ArticleCASPubMedPubMed Central Google Scholar
Altaf, M. et al. Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin. Mol. Cell28, 1002–1014 (2007). ArticleCASPubMedPubMed Central Google Scholar
van Leeuwen, F. & Gottschling, D.E. Assays for gene silencing in yeast. Methods Enzymol.350, 165–186 (2002). ArticleCASPubMed Google Scholar
Rusche, L.N., Kirchmaier, A.L. & Rine, J. The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae. Annu. Rev. Biochem.72, 481–516 (2003). ArticleCASPubMed Google Scholar
Ezhkova, E. & Tansey, W.P. Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol. Cell13, 435–442 (2004). ArticleCASPubMed Google Scholar
Zhang, X. et al. Structural basis for the product specificity of histone lysine methyltransferases. Mol. Cell12, 177–185 (2003). ArticlePubMedPubMed Central Google Scholar
Tamaru, H. et al. Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in Neurospora crassa. Nat. Genet.34, 75–79 (2003). ArticleCASPubMed Google Scholar
Patnaik, D. et al. Substrate specificity and kinetic mechanism of mammalian G9a histone H3 methyltransferase. J. Biol. Chem.279, 53248–53258 (2004). ArticleCASPubMed Google Scholar
Collins, R.E. et al. In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases. J. Biol. Chem.280, 5563–5570 (2005). ArticleCASPubMed Google Scholar
Dirk, L.M. et al. Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases. Biochemistry46, 3905–3915 (2007). ArticleCASPubMed Google Scholar
Eskeland, R. et al. The N-terminus of Drosophila SU(VAR)3–9 mediates dimerization and regulates its methyltransferase activity. Biochemistry43, 3740–3749 (2004). ArticleCASPubMed Google Scholar
Chin, H.G., Patnaik, D., Esteve, P.O., Jacobsen, S.E. & Pradhan, S. Catalytic properties and kinetic mechanism of human recombinant Lys-9 histone H3 methyltransferase SUV39H1: participation of the chromodomain in enzymatic catalysis. Biochemistry45, 3272–3284 (2006). ArticleCASPubMed Google Scholar
McBride, A.E. & Silver, P.A. State of the Arg: protein methylation at arginine comes of age. Cell106, 5–8 (2001). ArticleCASPubMed Google Scholar
Barski, A. et al. High-resolution profiling of histone methylations in the human genome. Cell129, 823–837 (2007). ArticleCASPubMed Google Scholar
Janzen, C.J., Hake, S.B., Lowell, J.E. & Cross, G.A. Selective di- or trimethylation of histone H3 lysine 76 by two DOT1 homologs is important for cell cycle regulation in Trypanosoma brucei. Mol. Cell23, 497–507 (2006). ArticleCASPubMed Google Scholar
Lee, J.S. et al. Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS. Cell131, 1084–1096 (2007). ArticleCASPubMed Google Scholar
Rappsilber, J., Ishihama, Y. & Mann, M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem.75, 663–670 (2003). ArticleCASPubMed Google Scholar
Krijgsveld, J., Gauci, S., Dormeyer, W. & Heck, A.J. In-gel isoelectric focusing of peptides as a tool for improved protein identification. J. Proteome Res.5, 1721–1730 (2006). ArticleCASPubMed Google Scholar