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acetyl+histone+h2a


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  • Single nucleosome ChIPs identify an extensive switch of acetyl marks on cell cycle promoters. 20505338

    Histones are modified by different post-translational modifications which are marks of peculiar chromatin functions. We previously evaluated histone methylations of G1/S and G2/M cell-cycle promoters at the single nucleosome level; here we report an analysis of acetylation marks, including some for which essentially nothing is known. In general, our data confirm the presence of H3/H4, but not H2A/H2B, in active core promoters. H3K14ac and H3K27ac are associated with active promoters, while H3K9ac and H3K18ac are more ambiguous, being also found under repression. Acetylation of H3K36, H3K79 and H2BK120, all residues involved in positive function through methylations or monoubiquitination, were found on repressed genes. H2Bub was present only on transcribed areas, and absent on core promoters or upstream nucleosomes. KAT2A/KAT2B and subunits of the SAGA and ATAC complexes have differential and dynamic roles: KAT2A-inactivated MEFs show a G1/S block, and KAT2B is important for G2/M. Furthermore, the precision of our analysis allows us to locate some acetylations specifically occurring upstream, downstream or in core promoters. Overall, the switch between methylations-and monoubiquitination-and acetylations on histone Lysines is a general theme on this dynamic group of genes.
    문서 타입:
    Reference
    카탈로그 번호:
    07-677
  • MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1. 20837706

    MOF (MYST1) is the major enzyme to catalyze acetylation of histone H4 lysine 16 (K16) and is highly conserved through evolution. Using a conditional knockout mouse model and the derived mouse embryonic fibroblast cell lines, we showed that loss of Mof led to a global reduction of H4 K16 acetylation, severe G(2)/M cell cycle arrest, massive chromosome aberration, and defects in ionizing radiation-induced DNA damage repair. We further showed that although early DNA damage sensing and signaling by ATM were normal in Mof-null cells, the recruitment of repair mediator protein Mdc1 and its downstream signaling proteins 53bp1 and Brca1 to DNA damage foci was completely abolished. Mechanistic studies suggested that Mof-mediated H4 K16 acetylation and an intact acidic pocket on H2A.X were essential for the recruitment of Mdc1. Removal of Mof and its associated proteins phenocopied a charge-neutralizing mutant of H2A.X. Given the well-characterized H4-H2A trans interactions in regulating higher-order chromatin structure, our study revealed a novel chromatin-based mechanism that regulates the DNA damage repair process.
    문서 타입:
    Reference
    카탈로그 번호:
    Multiple
    제품명:
    Multiple