Dot1p modulates silencing in yeast by methylation of the nucleosome core.

By F. van Leeuwen, Philip R. Gafken, D. Gottschling. Cell, 2002

884 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/a4df7713b6e12e120d4132eb62f89ce6786941ae

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In Molecular Biology

Citations in the corpus

Noncompetitive Counteractions of DNA Polymerase ε and ISW2/yCHRAC for Epigenetic Inheritance of Telomere Position Effect in Saccharomyces cerevisiae (2004, background): “Spreading of Sir proteins into the HM loci and subtelomeric DNA is probably facilitated by the interaction of Sir3/Sir4 with hypoacetylated histones H3/H4 and Sir2, a NAD-dependent histone deacetylase (14, 23, 24, 54), and blocked by Dot1-catalyzed methylation of histone H3 (33, 36, 42).”
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact (2012, neutral): “The second class of KMTs is represented solely by KMT4 (also known as Dot1p in yeast and Dot1L in human), which does not have a SET domain (Okada et al., 2005; van Leeuwen et al., 2002).”
Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. (2002, background): “With the exception of DOT1p (van Leeuwen et al., 2002),3 Correspondence: pirrotta@zoo.unige.ch all reported histone MTases that methylate lysine residues contain a SET domain, which harbors the amino acids important for MTase function.”
The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. (2004, background): “Methylation of Lys 79 of histone H3 was first described in Saccharomyces cerevisiae as a histone modification that occurs at the majority of nucleosomes and that can affect gene silencing even though it is absent from silenced loci (Ng et al. 2002; van Leeuwen et al. 2002).”
Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. (2005, neutral): “Methylations are not uniform throughout the genome, and specific modifications have been correlated with transcription activation or repression (Briggs et al., 2001; Krogan et al., 2002a, 2003c; Ng et al., 2002, 2003; van Leeuwen et al., 2002).”
An epigenetic road map for histone lysine methylation (2003, background): “…of histone lysine methylation At least five methylatable lysine positions exist in the N-termini of histones H3 (K4, K9, K27, K36) and H4 (K20); another occurs in the histone-fold domain of histone H3 (K79) (Feng et al., 2002; Lacoste et al., 2002; Ng et al., 2002; van Leeuwen et al., 2002).”
Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. (2003, background): “However, recent observations indicate that the deacetylase Hos2 is involved in transcriptional activation through histone targets, possibly to regenerate a permissive, low-acetylated chromatin ground state during multiple rounds of transcription (Wang et al. 2002).”
Histone variant H2A.Z marks the 5' ends of both active and inactive genes in euchromatin. (2005, background): “Z (Meneghini et al., 2003) and three histone modifications: acetylation on lysine 16 of the H4 tail (Kimura et al., 2002; Suka et al., 2002) and methylation of lysines 4 and 79 of H3 (Ng et al., 2003a; Santos-Rosa et al., 2004; van Leeuwen et al., 2002).”
Binary switches and modification cassettes in histone biology and beyond (2003, background): “, loss of silencing in yeast mutants of H3 Lys 79 and the corresponding HMT, Dot1, must be caused by indirect effect”