Histone H3K9Me3 (3-17) is an N-terminal peptide fragment of histone H3 that corresponds to amino acid residues 4-18 of the human histone H3 sequence. Trimethylation of histone H3 at lysine 9 is associated with gene repression, prevents transcription factor binding, and is a target of the heterochromatin protein 1 (HP1) family proteins CBX1, CBX3, and CBX5.1,2 It is recognized by the plant homeodomain fingers of chromodomain helicase DNA binding protein 4 (CHD4), a member of the NuRD deacetylase complex that is upregulated in a variety of cancers and implicated in the DNA damage response.3
References
1. Kaustov, L., Ouyang, H., Amaya, M., et al. Recognition and specificity determinants of the human Cbx chromodomains. J. Biol. Chem. 286(1), 521-529 (2011).
2. Becker, J.S., Nicetto, D., and Zaret, K.S. H3K9me3-dependent heterochromatin: Barrier to cell fate changes. Trends Genet. 32(1), 29-41 (2016).
3. Mansfield, R.E., Musselman, C.A., Kwan, A.H., et al. Plant homeodomain (PHD) fingers of CHD4 are histone H3-binding modules with preference for unmodified H3K4 and methylated H3K9. J. Biol. Chem. 286(13), 11779-11791 (2011).