H3K36me2

H3K36me2 refers to the di-methylation of lysine 36 on histone H3, a conserved post-translational modification associated with chromatin and gene regulation. This mark is distinct from H3K36me3 and is commonly studied in the context of transcriptional elongation and chromatin structure within gene bodies of active genes.

The addition and removal of H3K36me2 are carried out by specific enzymes. Histone methyltransferases of the NSD family, including NSD1 and NSD2 (also known as WHSC1 and WHSC1L1), are primarily implicated in depositing the di-methyl mark. Trimethylation at the same residue (H3K36me3) is typically performed by SETD2, providing a related but separate layer of regulation. Demethylation of H3K36me2 is carried out by demethylases such as KDM2A and KDM2B, among other potential enzymes, reflecting dynamic control of this modification in response to cellular conditions.

Genomically, H3K36me2 is enriched across the bodies of actively transcribed genes and plays a role in coordinating transcription elongation and chromatin organization. It can influence the recruitment of chromatin-modifying complexes, impact nucleosome density, and contribute to the regulation of splicing and genomic stability. The mark is also involved in maintaining proper chromatin states by limiting inappropriate transcription initiation within coding regions.

Biological and clinical relevance of H3K36me2 includes associations with developmental processes and cancer, where altered levels can reflect or contribute to changes in gene expression programs. Detection and study of H3K36me2 typically rely on chromatin immunoprecipitation followed by sequencing (ChIP-seq) using antibodies specific to the di-methyl mark.