Biology:HIST1H2AE
Generic protein structure example |
Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AE gene.[1][2][3][4]
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 lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.[4]
References
- ↑ "Human histone gene organization: nonregular arrangement within a large cluster". Genomics 40 (2): 314–22. Apr 1997. doi:10.1006/geno.1996.4592. PMID 9119399.
- ↑ "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics 10 (4): 940–8. Nov 1991. doi:10.1016/0888-7543(91)90183-F. PMID 1916825.
- ↑ "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–98. Oct 2002. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ↑ 4.0 4.1 "Entrez Gene: HIST1H2AE histone cluster 1, H2ae". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3012.
Further reading
- Rodriguez P; Munroe D; Prawitt D et al. (1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". Genomics 44 (3): 253–65. doi:10.1006/geno.1997.4868. PMID 9325046.
- "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. 1998. doi:10.1007/s004390050630. PMID 9439656.
- "Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter". Mol. Cell. Biol. 18 (5): 2535–44. 1998. doi:10.1128/mcb.18.5.2535. PMID 9566873.
- Deng L; de la Fuente C; Fu P et al. (2001). "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. doi:10.1006/viro.2000.0593. PMID 11080476.
- Deng L; Wang D; de la Fuente C et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
- Galasinski SC; Louie DF; Gloor KK et al. (2002). "Global regulation of post-translational modifications on core histones". J. Biol. Chem. 277 (4): 2579–88. doi:10.1074/jbc.M107894200. PMID 11709551.
- Strausberg RL; Feingold EA; Grouse LH et al. (2003). "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. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- Mungall AJ; Palmer SA; Sims SK et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
- "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". EMBO J. 22 (24): 6550–61. 2004. doi:10.1093/emboj/cdg631. PMID 14657027.
- "Phosphorylation of histone H2A inhibits transcription on chromatin templates". J. Biol. Chem. 279 (21): 21866–72. 2004. doi:10.1074/jbc.M400099200. PMID 15010469.
- Aihara H; Nakagawa T; Yasui K et al. (2004). "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo". Genes Dev. 18 (8): 877–88. doi:10.1101/gad.1184604. PMID 15078818.
- Wang H; Wang L; Erdjument-Bromage H et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing". Nature 431 (7010): 873–8. doi:10.1038/nature02985. PMID 15386022. Bibcode: 2004Natur.431..873W.
- Gerhard DS; Wagner L; Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes". Biochemistry 44 (15): 5827–34. 2005. doi:10.1021/bi047505c. PMID 15823041.
- Bonenfant D; Coulot M; Towbin H et al. (2006). "Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry". Mol. Cell. Proteomics 5 (3): 541–52. doi:10.1074/mcp.M500288-MCP200. PMID 16319397.
- "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing". Mol. Cell 20 (6): 845–54. 2006. doi:10.1016/j.molcel.2005.12.002. PMID 16359901.
- "Precise characterization of human histones in the H2A gene family by top down mass spectrometry". J. Proteome Res. 5 (2): 248–53. 2006. doi:10.1021/pr050269n. PMID 16457589.