Target type: molecularfunction
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H2A)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H2A)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to the arginine residue at position 3 of histone H2A. [GOC:mah, PMID:17898714, PMID:23451136]
Histone H2AR3 methyltransferase activity refers to the enzymatic ability to catalyze the transfer of a methyl group from a donor molecule, such as S-adenosyl methionine (SAM), to the arginine residue at position 3 (R3) of histone H2A. This methylation event specifically targets the N-terminal tail of histone H2A, a core component of the nucleosome, the fundamental unit of chromatin. Histone H2A is one of five major histone proteins that package DNA into chromatin, and its methylation at R3 plays a crucial role in regulating chromatin structure and function.
The methylation of H2AR3 is a dynamic process that can be modulated by various factors, including developmental stage, cellular environment, and external stimuli. This modification is associated with diverse biological processes, including gene expression, DNA replication, and repair.
Specifically, H2AR3 methylation can influence gene expression in several ways:
* **Chromatin compaction:** Methylation of H2AR3 has been shown to promote chromatin compaction, which can suppress gene expression by limiting the accessibility of transcription factors and other regulatory proteins to DNA.
* **Recruitment of specific proteins:** H2AR3 methylation can serve as a docking site for proteins that bind to methylated lysines, such as the Polycomb repressive complex 2 (PRC2). These proteins can further modify chromatin and influence gene expression.
* **Epigenetic regulation:** H2AR3 methylation is considered an epigenetic mark, as it can be inherited by daughter cells and contribute to the long-term regulation of gene expression.
The molecular mechanisms underlying the role of H2AR3 methylation in DNA replication and repair are less well understood, but studies have shown that this modification may be involved in the recruitment of DNA repair machinery to damaged DNA sites.
In summary, histone H2AR3 methyltransferase activity is a critical enzyme involved in regulating chromatin structure and function. Its activity influences gene expression, DNA replication, and repair through the methylation of H2AR3, a modification that serves as a crucial epigenetic mark and a regulatory signal for chromatin-associated processes.'
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Protein | Definition | Taxonomy |
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Protein arginine N-methyltransferase 6 | A protein arginine N-methyltransferase 6 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q96LA8] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
sulfathiazole | sulfathiazole : A 1,3-thiazole compound having a 4-aminobenzenesulfonamido group at the 2-position. Sulfathiazole: A sulfathiazole compound that is used as a short-acting anti-infective agent. It is no longer commonly used systemically due to its toxicity, but may still be applied topically in combination with other drugs for the treatment of vaginal and skin infections, and is still used in veterinary medicine. | 1,3-thiazoles; substituted aniline; sulfonamide; sulfonamide antibiotic | antiinfective agent; drug allergen; EC 2.5.1.15 (dihydropteroate synthase) inhibitor; environmental contaminant; xenobiotic |
c.i. direct red 23 | C.I. Direct Red 23: azo dye; structure in first source | ||
furamidine | furamidine: RN given refers to parent cpd; WR 199385 refers to di-HCl; pafuramidine is a prodrug of this | ||
stilbamidine | stilbamidine: RN given refers to parent cpd |