Identification of small molecules that inhibit the histone chaperone Asf1 and its chromatin function.
作者： Ja-Hwan Seol , Tae-Yang Song , Se Eun Oh , Chanhee Jo , Ahreum Choi
DOI: 10.5483/BMBREP.2015.48.12.063
关键词:
摘要: The eukaryotic genome is packed into chromatin, which important for the genomic integrity and gene regulation. Chromatin structures are maintained through assembly disassembly of nucleosomes catalyzed by histone chaperones. Asf1 (anti-silencing function 1) a highly conserved chaperone that mediates transfer on/off DNA promotes H3 lysine 56 acetylation at globular core domain H3. To elucidate role in modulation chromatin structure, we screened identified small molecules inhibit H3K56 without affecting other modifications. These pyrimidine-2,4,6-trione derivative inhibited nucleosome mediated vitro, reduced HeLa cells. Furthermore, production HSV viral particles was these compounds. As implicated integrity, cell proliferation, cancer, current inhibitor may offer an opportunity therapeutic development treatment diseases. [BMB Reports 2015; 48(12): 685-690]
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