Histone H2A.Z is a protein that in humans is encoded by the H2AFZgene.[1][2]
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. The H2AFZ gene encodes a replication-independent member of the histone H2A family that is distinct from other members of the family. Studies 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.[2]
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, in 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. Positioning of H2A.Z containing nucleosomes around transcription start sites has now been shown to affect the downstream gene expression.[3]
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.[4]
References
↑Hatch CL, Bonner WM (Oct 1990). "The human histone H2A.Z gene. Sequence and regulation". J Biol Chem. 265 (25): 15211–8. PMID1697587.
Jason LJ, Moore SC, Lewis JD, et al. (2002). "Histone ubiquitination: a tagging tail unfolds?". BioEssays. 24 (2): 166–74. doi:10.1002/bies.10038. PMID11835281.
Slachta CA, Jeevanandam V, Goldman B, et al. (2000). "Coronary arteries from human cardiac allografts with chronic rejection contain oligoclonal T cells: persistence of identical clonally expanded TCR transcripts from the early post-transplantation period (endomyocardial biopsies) to chronic rejection (coronary arteries)". J. Immunol. 165 (6): 3469–83. doi:10.4049/jimmunol.165.6.3469. PMID10975868.
Pasqualucci L, Neri A, Baldini L, et al. (2000). "BCL-6 mutations are associated with immunoglobulin variable heavy chain mutations in B-cell chronic lymphocytic leukemia". Cancer Res. 60 (20): 5644–8. PMID11059755.
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. PMID11080476.
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:10.1038/81971. PMID11101893.
Bräuninger A, Yang W, Wacker HH, et al. (2001). "B-cell development in progressively transformed germinal centers: similarities and differences compared with classical germinal centers and lymphocyte-predominant Hodgkin disease". Blood. 97 (3): 714–9. doi:10.1182/blood.V97.3.714. PMID11157489.
Yamamoto K, Sugita N, Kobayashi T, et al. (2001). "Evidence for a novel polymorphism affecting both N-linked glycosylation and ligand binding of the IgG receptor IIIB (CD16)". Tissue Antigens. 57 (4): 363–6. doi:10.1034/j.1399-0039.2001.057004363.x. PMID11380948.
Faast R, Thonglairoam V, Schulz TC, et al. (2001). "Histone variant H2A.Z is required for early mammalian development". Curr. Biol. 11 (15): 1183–7. doi:10.1016/S0960-9822(01)00329-3. PMID11516949.
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. PMID11689053.
