Understanding the language of Lys36 methylation at histone H3

By Eric J. Wagner, P. Carpenter. Nature reviews. Molecular cell biology, 2012

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Histone side chains are post-translationally modified at multiple sites, including at Lys36 on histone H3 (H3K36). Several enzymes from yeast and humans, including the methyltransferases SET domain-containing 2 (Set2) and nuclear receptor SET domain-containing 1 (NSD1), respectively, alter the methylation status of H3K36, and significant progress has been made in understanding how they affect chromatin structure and function. Although H3K36 methylation is most commonly associated with the transcription of active euchromatin, it has also been implicated in diverse processes, including alternative splicing, dosage compensation and transcriptional repression, as well as DNA repair and recombination. Disrupted placement of methylated H3K36 within the chromatin landscape can lead to a range of human diseases, underscoring the importance of this modification.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/948c36b1e94b1b36106fcb2f66ba17bc83a46341

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Citations in the corpus

Regulation of nucleosome dynamics by histone modifications (2013, neutral): “Similarly, enrichment of H3K36me2/3 over gene bodies is highly conserved 37 , but loss of the H3K36 methyltransferase Set2 has only minor effects on transcription 35 .”
Gene Body Methylation can alter Gene Expression and is a Therapeutic Target in Cancer (2014, background): “…transcription elongation H3K36m3, which we found to be enriched only in the fast remethylation group (group I), has been shown to suppress histone exchange on transcribed genes, thus maintaining the accuracy and efficiency of transcription (Venkatesh et al., 2012; Wagner and Carpenter, 2012).”
COMPREHENSIVE MOLECULAR CHARACTERIZATION OF CLEAR CELL RENAL CELL CARCINOMA (2013, background): “All rights reserved©2013 Kyle Chang1, Nipun Kakkar1, Lisa R. Treviño1, Susan Benton1, Jeffrey G. Reid1, Donna Morton1, Harsha Doddapaneni1, Yi Han1, Lora Lewis1, Huyen Dinh1, Christie Kovar1, Yiming Zhu1, Jireh Santibanez1, Min Wang1, Walker Hale1, Divya Kalra1, Chad J. Creighton1,2, David A. Wheel”
The interplay of histone modifications – writers that read (2015, positive): “Mammals on the other hand have multiple writers of H3K36 methylation, including the NSD1/2/3 family, ASH1L, SMYD2, SETMAR, and SETD2, but SETD2 is the sole enzyme responsible for H3K36 trimethylation in vivo (reviewed in [57]) (Fig 4).”