HIST1H3F
Histone H3.1 is a protein that in humans is encoded by the HIST1H3F gene.[1][2][3]
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 H3 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.[3]
References
References
- ↑ Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). “Human histone gene organization: nonregular arrangement within a large cluster”. Genomics. 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
- ↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). “The human and mouse replication-dependent histone genes”. Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ↑ 3.0 3.1 “Entrez Gene: HIST1H3F histone cluster 1, H3f”.
Further reading
Further reading
- Albig W, Kardalinou E, Drabent B, et al. (1991). “Isolation and characterization of two human H1 histone genes within clusters of core histone genes”. Genomics. 10 (4): 940–8. doi:10.1016/0888-7543(91)90183-F. PMID 1916825.
- Albig W, Doenecke D (1998). “The human histone gene cluster at the D6S105 locus”. Hum. Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
- El Kharroubi A, Piras G, Zensen R, Martin MA (1998). “Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter”. Mol. Cell. Biol. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
- Rea S, Eisenhaber F, O’Carroll D, et al. (2000). “Regulation of chromatin structure by site-specific histone H3 methyltransferases”. Nature. 406 (6796): 593–9. doi:10.1038/35020506. PMID 10949293.
- Hsu JY, Sun ZW, Li X, et al. (2000). “Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes”. Cell. 102 (3): 279–91. doi:10.1016/S0092-8674(00)00034-9. PMID 10975519.
- 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.
- Lachner M, O’Carroll D, Rea S, et al. (2001). “Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins”. Nature. 410 (6824): 116–20. doi:10.1038/35065132. PMID 11242053.
- 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.
- Yang L, Xia L, Wu DY, et al. (2002). “Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor”. Oncogene. 21 (1): 148–52. doi:10.1038/sj.onc.1204998. PMID 11791185.
- 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. PMC 139241. PMID 12477932.
- Xiao B, Jing C, Wilson JR, et al. (2003). “Structure and catalytic mechanism of the human histone methyltransferase SET7/9”. Nature. 421 (6923): 652–6. doi:10.1038/nature01378. PMID 12540855.
- Koessler H, Doenecke D, Albig W (2003). “Aberrant expression pattern of replication-dependent histone h3 subtype genes in human tumor cell lines”. DNA Cell Biol. 22 (4): 233–41. doi:10.1089/104454903321908629. PMID 12823900.
- Lusic M, Marcello A, Cereseto A, Giacca M (2004). “Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter”. EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
- Couture JF, Collazo E, Hauk G, Trievel RC (2006). “Structural basis for the methylation site specificity of SET7/9”. Nat. Struct. Mol. Biol. 13 (2): 140–6. doi:10.1038/nsmb1045. PMID 16415881.
- Ewing RM, Chu P, Elisma F, et al. (2007). “Large-scale mapping of human protein-protein interactions by mass spectrometry”. Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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