Back to your search result

Description

Histone H3.1t (UniProt: Q16695, also known as H3/t, H3t, H3/g) is encoded by the HIST3H3 (also known as H3FT) gene (Gene ID: 8290) in human. Histones are highly conserved basic nuclear proteins that are responsible for the nucleosome structure of chromatin in eukaryotes. They play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which DNA is wrapped in repeating units, called nucleosomes, which limits DNA accessibility to the cellular machineries that require DNA as a template. Histone H3 features a main globular domain and a long N-terminal tail, which protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. The amino-terminal tails of histone proteins are subject to posttranslational modifications, including acetylation and methylation, which recruit downstream regulatory factors, influence chromatin structure, and are critical determinants of transcription. Acetylation of histone H3 occurs at several different lysine positions in the histone tail and is performed by a family histone acetyltransferases. Acetylation is generally associated with transcriptional activity and methylation of lysine and arginine residues can either activate or repress depending on the residue modified. There is a significant correlation between acetylation of histones H3 in promoter regions and transcriptional activity. The presence of H3K4me3 has been correlated with transcriptionally active promoters of genes and its levels positively correlate with gene expression levels. H3K4me3 has been implicated in a number of nuclear processes, including Pol II-mediated transcription, pre-mRNA splicing, DNA recombination, and DNA repair. Histaminylation of glutamine 5 on histone H3 (H3Q5Histaminyl) is recently identified as a permissive post-translational modification that coexists with adjacent lysine 4 trimethylation. (Ref.: Zhao, S., et al. (2021). Proc. Natl. Acad. Sci. USA. 118(6):e2016742118, Diehl?, KL., and Muir, TW. (2020). Nat. Chem. Biol. 16, 620-629, Bernstein, BE., et al. (2002). Proc. Natl. Acad. Sci. USA. 99(13),8695-8700).