Les histones sont des protéines nucléaires de base responsables de la structure nucléosomale de la fibre chromosomique chez les eucaryotes. Les nucléosomes consistent en environ 146 pb d'ADN enroulé autour d'un octamère d'histone composé de paires de chacune des quatre histones principales (H2A, H2B, H3 et H4). La fibre de chromatine est ensuite compactée par l'interaction d'une histone de liaison, H1, avec l'ADN inter-nucléosomal pour former des structures de chromatine d'ordre supérieur. Ce gène code un membre de la famille des histones H2A. Il s'agit d'un variant d'histone qui remplace les histones H2A conventionnelles dans un sous-ensemble de nucléosomes où il réprime la transcription et participe à l'inactivation stable du chromosome X.L'épissage alternatif de ce transcrit résulte en plusieurs variants de transcription codant différentes isoformes. L'expression de ces isoformes est associée à plusieurs cancers, tels que le carcinome hépatocellulaire.
↑«Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning», Proceedings of the National Academy of Sciences of the United States of America, vol.95, no14, , p.8175–80 (PMID9653160, PMCID20949, DOI10.1073/pnas.95.14.8175)
El Kharroubi A, Piras G, Zensen R, Martin MA, «Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter», Molecular and Cellular Biology, vol.18, no5, , p.2535–44 (PMID9566873, PMCID110633, DOI10.1128/mcb.18.5.2535)
Costanzi C, Pehrson JR, «Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals», Nature, vol.393, no6685, , p.599–601 (PMID9634239, DOI10.1038/31275)
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z, «Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells», Genome Research, vol.10, no10, , p.1546–60 (PMID11042152, PMCID310934, DOI10.1101/gr.140200)
Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F, «Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones», Virology, vol.277, no2, , p.278–95 (PMID11080476, DOI10.1006/viro.2000.0593)
Chadwick BP, Willard HF, «Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant», Human Molecular Genetics, vol.10, no10, , p.1101–13 (PMID11331621, DOI10.1093/hmg/10.10.1101)
Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F, «Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA», Virology, vol.289, no2, , p.312–26 (PMID11689053, DOI10.1006/viro.2001.1129)
Chadwick BP, Willard HF, «Cell cycle-dependent localization of macroH2A in chromatin of the inactive X chromosome», The Journal of Cell Biology, vol.157, no7, , p.1113–23 (PMID12082075, PMCID2173542, DOI10.1083/jcb.200112074)
Takahashi I, Kameoka Y, Hashimoto K, «MacroH2A1.2 binds the nuclear protein Spop», Biochimica et Biophysica Acta, vol.1591, nos1-3, , p.63–8 (PMID12183056, DOI10.1016/S0167-4889(02)00249-5)
Ganesan S, Silver DP, Greenberg RA, Avni D, Drapkin R, Miron A, Mok SC, Randrianarison V, Brodie S, Salstrom J, Rasmussen TP, Klimke A, Marrese C, Marahrens Y, Deng CX, Feunteun J, Livingston DM, «BRCA1 supports XIST RNA concentration on the inactive X chromosome», Cell, vol.111, no3, , p.393–405 (PMID12419249, DOI10.1016/S0092-8674(02)01052-8)
Angelov D, Molla A, Perche PY, Hans F, Côté J, Khochbin S, Bouvet P, Dimitrov S, «The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling», Molecular Cell, vol.11, no4, , p.1033–41 (PMID12718888, DOI10.1016/S1097-2765(03)00100-X)
Behrends U, Schneider I, Rössler S, Frauenknecht H, Golbeck A, Lechner B, Eigenstetter G, Zobywalski C, Müller-Weihrich S, Graubner U, Schmid I, Sackerer D, Späth M, Goetz C, Prantl F, Asmuss HP, Bise K, Mautner J, «Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries», International Journal of Cancer, vol.106, no2, , p.244–51 (PMID12800201, DOI10.1002/ijc.11208)
Lusic M, Marcello A, Cereseto A, Giacca M, «Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter», The EMBO Journal, vol.22, no24, , p.6550–61 (PMID14657027, PMCID291826, DOI10.1093/emboj/cdg631)
Acín-Pérez R, Bayona-Bafaluy MP, Fernández-Silva P, Moreno-Loshuertos R, Pérez-Martos A, Bruno C, Moraes CT, Enríquez JA, «Respiratory complex III is required to maintain complex I in mammalian mitochondria», Molecular Cell, vol.13, no6, , p.805–15 (PMID15053874, PMCID3164363, DOI10.1016/S1097-2765(04)00124-8)
Zhang R, Poustovoitov MV, Ye X, Santos HA, Chen W, Daganzo SM, Erzberger JP, Serebriiskii IG, Canutescu AA, Dunbrack RL, Pehrson JR, Berger JM, Kaufman PD, Adams PD, «Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA», Developmental Cell, vol.8, no1, , p.19–30 (PMID15621527, DOI10.1016/j.devcel.2004.10.019)
Hernández-Muñoz I, Lund AH, van der Stoop P, Boutsma E, Muijrers I, Verhoeven E, Nusinow DA, Panning B, Marahrens Y, van Lohuizen M, «Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase», Proceedings of the National Academy of Sciences of the United States of America, vol.102, no21, , p.7635–40 (PMID15897469, PMCID1140410, DOI10.1073/pnas.0408918102)
Ioudinkova ES, Barat A, Pichugin A, Markova E, Sklyar I, Pirozhkova I, Robin C, Lipinski M, Ogryzko V, Vassetzky YS, Razin SV, «Distinct distribution of ectopically expressed histone variants H2A.Bbd and MacroH2A in open and closed chromatin domains», PLOS ONE, vol.7, no10, , e47157 (PMID23118866, PMCID3484066, DOI10.1371/journal.pone.0047157)