Histone methyltransferase: Difference between revisions
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== Function == | == Function == | ||
'''Histone methyltransferase''' (HMT) are '''histone-lysine N-methyltransferase''' (KHMT) and '''histone-arginine N-methyltransferase''' (RHMT) which catalyzes the transfer of methyl groups to lysine and arginine residues of histones<ref>PMID:15248813</ref>. HMT use S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) as the methyl donor. KHMT can be SET domain-containing or non-SET domain-containing. The SET domain contains the catalytic core of KHMT and targets the lysine tail region of KHMT. CxxC domain is a zinc finger domain. | '''Histone methyltransferase''' (HMT) are '''histone-lysine N-methyltransferase''' (KHMT) and '''histone-arginine N-methyltransferase''' (RHMT) which catalyzes the transfer of methyl groups to lysine and arginine residues of histones<ref>PMID:15248813</ref>. HMT use S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) as the methyl donor. KHMT can be SET domain-containing or non-SET domain-containing. The SET domain contains the catalytic core of KHMT and targets the lysine tail region of KHMT. CxxC domain is a zinc finger domain. | ||
For SET7/9 see [[Histone Lysine Methyltransferase SET7/9]]. | |||
== Relevance == | == Relevance == | ||
Revision as of 13:28, 10 February 2021
FunctionHistone methyltransferase (HMT) are histone-lysine N-methyltransferase (KHMT) and histone-arginine N-methyltransferase (RHMT) which catalyzes the transfer of methyl groups to lysine and arginine residues of histones[1]. HMT use S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) as the methyl donor. KHMT can be SET domain-containing or non-SET domain-containing. The SET domain contains the catalytic core of KHMT and targets the lysine tail region of KHMT. CxxC domain is a zinc finger domain. For SET7/9 see Histone Lysine Methyltransferase SET7/9. RelevanceInhibitors of the histone-lysine N-methyltransferase SMYD2 which represses the tumor-suppressing activities of p53 are studied as cancer therapy drugs[2]. DiseaseAberrant HMT plays a role in cancer, intellectual disability syndromes and regulation of tissue aging[3]. Structural highlightsHuman inserted in a hydrophobic environment[4]. Water molecules shown as red spheres 3D Structures of histone methyltransferaseHistone methyltransferase 3D structures
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ReferencesReferences
- ↑ Trievel RC. Structure and function of histone methyltransferases. Crit Rev Eukaryot Gene Expr. 2004;14(3):147-69. PMID:15248813
- ↑ Ferguson AD, Larsen NA, Howard T, Pollard H, Green I, Grande C, Cheung T, Garcia-Arenas R, Cowen S, Wu J, Godin R, Chen H, Keen N. Structural Basis of Substrate Methylation and Inhibition of SMYD2. Structure. 2011 Jul 20. PMID:21782458 doi:10.1016/j.str.2011.06.011
- ↑ Greer EL, Shi Y. Histone methylation: a dynamic mark in health, disease and inheritance. Nat Rev Genet. 2012 Apr 3;13(5):343-57. doi: 10.1038/nrg3173. PMID:22473383 doi:http://dx.doi.org/10.1038/nrg3173
- ↑ Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature. 2003 Feb 6;421(6923):652-6. Epub 2003 Jan 22. PMID:12540855 doi:10.1038/nature01378