Chemistry:Methyllysine
Methyllysine is derivative of the amino acid residue lysine where the sidechain ammonium group has been methylated one or more times.[1]
Such methylated lysines play an important role in epigenetics; the methylation of specific lysines of certain histones in a nucleosome alters the binding of the surrounding DNA to those histones, which in turn affects the expression of genes on that DNA.[2][3] The binding is affected because the effective radius of the positive charge is increased (methyl groups are larger than the hydrogen atoms they replace), reducing the strongest potential electrostatic attraction with the negatively charged DNA.
It is thought that the methylation of lysine (and arginine) on histone tails does not directly affect their binding to DNA. Rather, such methyl marks recruit other proteins that modulate chromatin structure.[4]
In Protein Data Bank files, methylated lysines are indicated by the MLY or MLZ acronyms.
Unmethylated lysine
Monomethylated: 6-N-methyllysine
Dimethylated: (6-N,6-N)dimethyllysine
Trimethylated: (6-N,6-N,6-N)trimethyllysine
References
- ↑ Hyun, Kwangbeom; Jeon, Jongcheol; Park, Kihyun; Kim, Jaehoon (2017). "Writing, erasing and reading histone lysine methylations". Experimental & Molecular Medicine 49 (4): e324. doi:10.1038/emm.2017.11. PMID 28450737.
- ↑ "Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark". Molecular Cell 25 (1): 15–30. January 2007. doi:10.1016/j.molcel.2006.12.014. PMID 17218268.
- ↑ "Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains". Genes & Development 17 (15): 1870–81. August 2003. doi:10.1101/gad.1110503. PMID 12897054.
- ↑ "Epigenetic protein families: a new frontier for drug discovery". Nature Reviews. Drug Discovery 11 (5): 384–400. April 2012. doi:10.1038/nrd3674. PMID 22498752.
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