Histone H3K36Me3 (31-41) is a peptide fragment of histone H3 that corresponds to amino acid residues 32-42 of the human histone H3.3 sequence. Unlike histone H3.1 and H3.2, the histone H3.3 variant contains a serine residue at position 31 that is phosphorylated during late prometaphase and metaphase of mitosis.1 Trimethylation of H3K36 is increased in the G1 and early S phases of the cell cycle where it binds to and recruits the mismatch recognition protein MutSα in preparation for DNA replication and mismatch repair.2 H3K36 trimethylation is found in greater amounts on exons compared with introns in C. elegans, mouse, and human genome-wide maps of histone H3 tail methylations.3
References
1. Hake, S.B., Garcia, B.A., Kauer, M., et al. Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes. Proc. Natl. Acad. Sci. U.S.A. 102(18), 6344-6349 (2005).
2. Li, F., Mao, G., Tong, D., et al. The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSα. Cell 153(3), 590-600 (2013).
3. Kolasinska-Zwierz, P., Down, T., Latorre, I., et al. Differential chromatin marking of introns and expressed exons by H3K36me3. Nat. Genet. 41(3), 376-381 (2009).