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Description

Histone H2A type 1 (UniProt: P0C0S8, also known as H2A.1, Histone H2A/p) is encoded by the HIST1H2AG (also known as HIST1H2AG, H2AFP, HIST1H2AI, H2AFC) gene (Gene ID: 8329, 8320, 8332, 8336, 8369) in human. Histone H2A is one of four components of the core nucleosomal structure. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Histones undergo a number of post-translational modifications (PTM) in response to various stimuli that serve important functions for regulation of gene expression, DNA repair, and chromatin. Histone H2A, in particular, undergoes acetylation on selected lysines, which may promote unfolding of chromatin and transcription. It can also be phosphorylated on selected serine residues, which mark mitosis and gene repression, or DNA damage. Arginine methylation is a less explored histone post-translational modification. It has been implicated in embryonic development, somatic transcriptional regulation, and cancer development. H2A arginine 3 methylation (R3me1, R3me2s, and R3me2a) is catalyzed by PRMT1 and PRMT5 in vitro. H2A methylation is shown to appear late in oogenesis and is most abundant in the laid egg. Arginine methylations are constrained to pre-mid blastula transition events in the embryo and are considered to be involved in the global transcriptional repression during development. H2A R3me2s is reported to be enriched on nucleosomes containing both active and repressive histone post-translational modifications in human A549 cells and Xenopus embryos. (Ref.: Wilczek, C et al. (2011). J Biol Chem. 286(49):42221-31, Wang, WL et al. (2014). BMC Epigenetics & Chromatin 7:22).