Histone H2A.Z
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Histone H2A.Z is a protein encoded by the H2AZ1 gene in humans.
Function Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 base pairs(bp) of DNA wrapped around a histone octamer, which includes pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted by the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. The H2AFZ gene encodes a replication-independent member of the histone H2A family that is distinct from other members of the family. Biological ImportanceStudies in mice have shown that this particular histone is required for embryonic development and indicate that lack of functional histone H2A leads to embryonic lethality.
Histone H2AZ is a variant of histone H2A, and is used to mediate the thermosensory response, and is essential to perceive the ambient temperature. Nucleosome occupancy of H2A.Z decreases with temperature, and in vitro assays show that H2A.Z-containing nucleosomes wrap DNA more tightly than canonical H2A nucleosomes in Arabidopsis.(Cell 140: 136–147, 2010) However, some of the other studies (Nat. Genet. 41, 941–945 and Genes Dev., 21, 1519–1529) have shown that incorporation of H2A.Z in nucleosomes, when it co-occurs with H3.3, makes them weaker.
Gene Expression and Chromatin Structure
The positioning of H2A.Z containing nucleosomes around transcription start sites has been shown to affect the downstream gene expression. Recent evidence also points to a role for H2A.Z in repressing a subset of ncRNAs, derepressing CUTs, as well as mediation higher order chromatin structure formation.
Further reading
- Jason LJ, Moore SC, Lewis JD, etal. (2002). "Histone ubiquitination: a tagging tail unfolds?". BioEssays. 24 (2): 166–74. doi:. PMID. S2CID.
- Hatch CL, Bonner WM (1988). . Nucleic Acids Res. 16 (3): 1113–24. doi:. PMC. PMID.
- Kato S, Sekine S, Oh SW, etal. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:. PMID.
- Hatch CL, Bonner WM (1995). . DNA Cell Biol. (Submitted manuscript). 14 (3): 257–66. doi:. PMID.
- Popescu N, Zimonjic D, Hatch C, Bonner W (1994). . Genomics (Submitted manuscript). 20 (2): 333–5. doi:. PMID.
- Hatch CL, Bonner WM (1996). "An upstream region of the H2AZ gene promoter modulates promoter activity in different cell types". Biochim. Biophys. Acta. 1305 (1–2): 59–62. doi:. PMID.
- El Kharroubi A, Piras G, Zensen R, Martin MA (1998). . Mol. Cell. Biol. 18 (5): 2535–44. doi:. PMC. PMID.
- Slachta CA, Jeevanandam V, Goldman B, etal. (2000). . J. Immunol. 165 (6): 3469–83. doi:. PMID.
- Pasqualucci L, Neri A, Baldini L, etal. (2000). "BCL-6 mutations are associated with immunoglobulin variable heavy chain mutations in B-cell chronic lymphocytic leukemia". Cancer Res. 60 (20): 5644–8. PMID.
- Deng L, de la Fuente C, Fu P, etal. (2001). . Virology. 277 (2): 278–95. doi:. PMID.
- Suto RK, Clarkson MJ, Tremethick DJ, Luger K (2001). "Crystal structure of a nucleosome core particle containing the variant histone H2A.Z". Nat. Struct. Biol. 7 (12): 1121–4. doi:. PMID. S2CID.
- Bräuninger A, Yang W, Wacker HH, etal. (2001). . Blood. 97 (3): 714–9. doi:. PMID.
- Yamamoto K, Sugita N, Kobayashi T, etal. (2001). . Tissue Antigens. 57 (4): 363–6. doi:. PMID.
- Faast R, Thonglairoam V, Schulz TC, etal. (2001). . Curr. Biol. 11 (15): 1183–7. Bibcode:. doi:. PMID.
- Deng L, Wang D, de la Fuente C, etal. (2001). . Virology. 289 (2): 312–26. doi:. PMID.
- Strausberg RL, Feingold EA, Grouse LH, etal. (2003). . Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:. doi:. PMC. PMID.
- Rangasamy D, Berven L, Ridgway P, Tremethick DJ (2003). . EMBO J. 22 (7): 1599–607. doi:. PMC. PMID.
- Lusic M, Marcello A, Cereseto A, Giacca M (2004). . EMBO J. 22 (24): 6550–61. doi:. PMC. PMID.
External links
- provides an overview of all the structure information available in the PDB for Human Histone H2A.Z