Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex.

By M. Keogh, S. Kurdistani, S. Morris, S. Ahn, V. Podolny, Sean R. Collins, Maya Schuldiner, Kayu Chin, Thanuja Punna, Natalie J. Thompson and 9 more. Cell, 2005

850 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3e74ca6f0cd0c2ffdc93bff93cd956f8382a0e82

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In Molecular Biology

1. Yang Shi
2. Keji Zhao
3. Kairong Cui
4. J. Whetstine
5. Yi Zhang
6. Dustin E. Schones
7. A. Shilatifard
8. K. Helin

Citations in the corpus

• The interplay of histone modifications – writers that read (2015, neutral): “In yeast, recognition of H3K36me2/3 by the bromodomain-containing EAF3 complex recruits the HDAC RPD3S complex, which deacetylates histones and prevents spurious transcription initiation from within gene bodies [61–63].”
• Long noncoding RNAs: functional surprises from the RNA world. (2009, background): “This is because transcriptional elongation causes histone marks to be added that prevent ‘‘spurious’’ transcription initiation from sites within the body of the transcript (Carrozza et al. 2005; Joshi and Struhl 2005; Keogh et al. 2005).”
• Covalent modifications of histones during development and disease pathogenesis (2007, neutral): “Through this association, Rpd3S has been implicated in preventing inappropriate initiation within the protein-coding region of actively transcribed gene”
• The role of chromatin during transcription. (2007, background): “Trimethylation leads to the recruitment of Rpd3S and creates a hypoacetylated environment within ORFs (Carrozza et al., 2005; Joshi and Struhl, 2005; Keogh et al., 2005).”
• The RNA polymerase II CTD coordinates transcription and RNA processing. (2012, background): “Rpd3S then transfers to H3 by interaction of the Eaf3 and Rco subunits with methylated H3K36, which is required for activation of acetylation activity (Drouin et al. 2010; Govind et al. 2010).”
• Regulation of histone methylation by demethylimination and demethylation (2007, background): “H3K36 methylation within the body of active genes recruits transcriptional repressors to suppress the initiation of intragenic transcription 68–70 .”
• Reading protein modifications with interaction domains (2006, background): “Methylated Lys36 of histone H3, in turn, might regulate transcription by recruiting the chromodomain of a histone deacetylase comple”
• Differential chromatin marking of introns and expressed exons by H3K36me3 (2009, background): “There is evidence that one function of H3K36me3 in the gene body is to prevent aberrant transcription initiatio”
• Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, background): “Whereas the H3K36me3/me2 mark is associated with transcriptional elongation (Joshi and Struhl 2005; Keogh et al. 2005; Lee and Shilatifard 2007) and possibly fulfills important roles in suppression of inappropriate transcription within the body of genes (Carrozza et al.”
• Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes (2009, background): “It has been shown that the Rpd3-containing complexes recruited by the H3K36 methylation signals after the RNA Pol II passage can deacetylate histones and prevent cryptic transcriptional initiation in yeast (Carrozza et al., 2005; Joshi and Struhl, 2005; Keogh et al., 2005).”
• DNA transposons and the evolution of eukaryotic genomes. (2007, neutral): “spurious intragenic transcription (25, 99).”
• Understanding the language of Lys36 methylation at histone H3 (2012, neutral): “Set2 catalyses H3K36 methylation co-transcriptionally and recruits the reduced potassium dependency 3 small (Rpd3S) deacetylase complex her”