H2AZ1
Histon H2A.Z jest protein koji je kod ljudi kodiran genom H2AZ1 sa hromosoma 4.[5][6]
Aminokiselinska sekvenca
Dužina polipeptidnog lanca je 128 aminokiseline, a molekulska težina 13.553 Da.[6]
10 | 20 | 30 | 40 | 50 | ||||
---|---|---|---|---|---|---|---|---|
MAGGKAGKDS | GKAKTKAVSR | SQRAGLQFPV | GRIHRHLKSR | TTSHGRVGAT | ||||
AAVYSAAILE | YLTAEVLELA | GNASKDLKVK | RITPRHLQLA | IRGDEELDSL | ||||
IKATIAGGGV | IPHIHKSLIG | KKGQQKTV |
Funkcija
Histoni su osnovni jedarni proteini koji su odgovorni za nukleosomsku strukturu hromosomskih vlakana u eukariotima. Nukleozomi se sastoje od približno 146 bp DNK omotane oko histonskih oktamera sastavljenog od parova svakog od četiri histonska jezgra (H2A, H2B, H3 i H4). Hromatinsko vlakno se dalje sabija kroz interakciju histonskih linkera, H1, sa DNK između nukleosoma kako bi se formirale strukture hromatina višeg reda. H2AFZ gen kodira replikaciju nezavisnog člana porodice histona H2A koji se razlikuje od ostalih članova porodice. Studije na miševima su pokazale da je ovaj histon neophodan za razvoj embriona i ukazuju da nedostatak funkcionalnog histona H2A dovodi do embrionske letalnosti.[6]
Histon H2AZ je varijanta histona H2A, i koristi se za posredovanje termosenzornog odgovora i neophodan je za percepciju temperature okoline. Zauzetost nukleosoma H2A.Z smanjuje se s temperaturom, a in vitro testovi pokazuju da nukleosomi koji sadrže H2A.Z čvršće obavijaju DNK od kanonskih nukleosoma H2A u Arabidopsis. Druge studije (Nat. Genet. 41, 941–945 i Genes Dev., 21, 1519–1529) pokazale su da ugradnja H2A.Z u nukleosome, kada se javlja zajedno sa H3.3, čini ih slabijima. Sada se pokazalo da pozicioniranje nukleosoma koji sadrže H2A.Z oko mjesta početka transkripcije utiče nizvodno na ekspresiju gena.[7]
Nedavni dokazi također ukazuju na ulogu H2A.Z u potiskivanju podskupa ncRNK, derepresiji CUT-a, kao i posredovanju u formiranju strukture hromatina višeg reda.[8]
Reference
- ^ a b c GRCh38: Ensembl release 89: ENSG00000164032 - Ensembl, maj 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037894 - Ensembl, maj 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Hatch CL, Bonner WM (Oct 1990). "The human histone H2A.Z gene. Sequence and regulation". J Biol Chem. 265 (25): 15211–8. doi:10.1016/S0021-9258(18)77243-8. PMID 1697587.
- ^ a b c "Entrez Gene: H2AFZ H2A histone family, member Z".
- ^ Bargaje R., Alam P., Patowary A., Sarkar M., Ali T., Gupta S., Garg M., Singh M., Purkanti R., Scaria V., Sivasubbu S., Brahmachari V., Pillai B. (2012) Proximity of H2A.Z containing nucleosome to the transcription start site influences gene expression levels in the mammalian liver and brain. Nucleic Acids Research (Epub ahead of print)Bargaje R, Alam MP, Patowary A, et al. (October 2012). "Proximity of H2A.Z containing nucleosome to the transcription start site influences gene expression levels in the mammalian liver and brain". Nucleic Acids Research. 40 (18): 8965–78. doi:10.1093/nar/gks665. PMC 3467062. PMID 22821566.
- ^ Rege M (2015). "Chromatin Dynamics and the RNA Exosome Function in Concert to Regulate Transcriptional Homeostasis". Cell Reports. 13 (8): 1610–1622. doi:10.1016/j.celrep.2015.10.030. PMC 4662874. PMID 26586442.
Dopunska litratura
- 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. PMID 11835281. S2CID 39905043.
- Hatch CL, Bonner WM (1988). "Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but highly conserved basal histone H2A isoprotein species". Nucleic Acids Res. 16 (3): 1113–24. doi:10.1093/nar/16.3.1113. PMC 334740. PMID 3344202.
- Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
- Hatch CL, Bonner WM (1995). "Characterization of the proximal promoter of the human histone H2A.Z gene". DNA Cell Biol. (Submitted manuscript). 14 (3): 257–66. doi:10.1089/dna.1995.14.257. PMID 7880446.
- Popescu N, Zimonjic D, Hatch C, Bonner W (1994). "Chromosomal mapping of the human histone gene H2AZ to 4q24 by fluorescence in situ hybridization". Genomics (Submitted manuscript). 20 (2): 333–5. doi:10.1006/geno.1994.1182. PMID 8020992.
- 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:10.1016/0167-4781(95)00223-5. PMID 8605251.
- 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.
- 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. PMID 10975868.
- 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. PMID 11059755.
- 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.
- 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. PMID 11101893. S2CID 5966635.
- 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. PMID 11157489.
- 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. PMID 11380948.
- 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. PMID 11516949.
- 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.
- 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Rangasamy D, Berven L, Ridgway P, Tremethick DJ (2003). "Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development". EMBO J. 22 (7): 1599–607. doi:10.1093/emboj/cdg160. PMC 152904. PMID 12660166.
- 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.
Vanjski linkovi
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Histone H2A.Z