HIST3H2A explained
Histone H2A type 3 is a protein that in humans is encoded by the HIST3H2A gene.[1]
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene contain a palindromic termination element.[2]
Further reading
- El Kharroubi A, Piras G, Zensen R, Martin MA . Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter . Mol. Cell. Biol. . 18 . 5 . 2535–44 . 1998 . 9566873 . 10.1128/mcb.18.5.2535. 110633 .
- Deng L, de la Fuente C, Fu P, etal . Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones . Virology . 277 . 2 . 278–95 . 2001 . 11080476 . 10.1006/viro.2000.0593 . free .
- Deng L, Wang D, de la Fuente C, etal . Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA . Virology . 289 . 2 . 312–26 . 2001 . 11689053 . 10.1006/viro.2001.1129 . free .
- Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
- Lusic M, Marcello A, Cereseto A, Giacca M . Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter . EMBO J. . 22 . 24 . 6550–61 . 2004 . 14657027 . 10.1093/emboj/cdg631 . 291826 .
- Zhang Y, Griffin K, Mondal N, Parvin JD . Phosphorylation of histone H2A inhibits transcription on chromatin templates . J. Biol. Chem. . 279 . 21 . 21866–72 . 2004 . 15010469 . 10.1074/jbc.M400099200 . free .
- Aihara H, Nakagawa T, Yasui K, etal . Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo . Genes Dev. . 18 . 8 . 877–88 . 2004 . 15078818 . 10.1101/gad.1184604 . 395847 .
- Wang H, Wang L, Erdjument-Bromage H, etal . Role of histone H2A ubiquitination in Polycomb silencing . Nature . 431 . 7010 . 873–8 . 2004 . 15386022 . 10.1038/nature02985 . 2004Natur.431..873W . 4344378 .
- Gerhard DS, Wagner L, Feingold EA, etal . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
- Hagiwara T, Hidaka Y, Yamada M . Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes . Biochemistry . 44 . 15 . 5827–34 . 2005 . 15823041 . 10.1021/bi047505c .
- Rual JF, Venkatesan K, Hao T, etal . Towards a proteome-scale map of the human protein-protein interaction network . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . 2005Natur.437.1173R . 4427026 .
- Cao R, Tsukada Y, Zhang Y . Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing . Mol. Cell . 20 . 6 . 845–54 . 2006 . 16359901 . 10.1016/j.molcel.2005.12.002 . free .
- Bergink S, Salomons FA, Hoogstraten D, etal . DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A . Genes Dev. . 20 . 10 . 1343–52 . 2006 . 16702407 . 10.1101/gad.373706 . 1472908 .
- Gregory SG, Barlow KF, McLay KE, etal . The DNA sequence and biological annotation of human chromosome 1 . Nature . 441 . 7091 . 315–21 . 2006 . 16710414 . 10.1038/nature04727 . 2006Natur.441..315G . free .
Notes and References
- Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ . The human and mouse replication-dependent histone genes . Genomics . 80 . 5 . 487–98 . Oct 2002 . 12408966 . 10.1016/S0888-7543(02)96850-3 .
- Web site: Entrez Gene: HIST3H2A histone cluster 3, H2a.