Histone methyltransferase
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Histone_methyltransferase".

Histone methyltransferases (HMT) are enzymes, histone-lysine N-methyltransferase and histone-arginine N-methyltransferase, which catalyze the transfer of one to three methyl groups from the cofactor S-Adenosyl methionine to lysine and arginine residues of histone proteins. These proteins often contain an SET (Su(var)3-9, Enhancer of Zeste, Trithorax) domain, however the recently discovered HMT Dot1 lacks the characteristic SET domain.

Histone methylation serves in epigenetic gene regulation. Methylated histones bind DNA more tightly, which inhibits transcription.

See also

• Histone-Modifying Enzymes
• Histone acetyltransferase
• Histone deacetylase
• RNA polymerase control by chromatin structure

Methylated histones can either repress or activate transcription as different experimental findings suggest.

External links

• MeSH Histone-Lysine+N-Methyltransferase
• MeSH Protein-Arginine+N-Methyltransferase

This transferase article is a stub. You can help Wikipedia by expanding it.