组蛋白
染色质
表观遗传学
计算生物学
生物
核小体
组蛋白甲基转移酶
组蛋白密码
组蛋白甲基化
表观遗传学
效应器
遗传学
DNA
组蛋白H2A
细胞生物学
基因
基因表达
DNA甲基化
作者
Catherine A. Musselman,Marie‐Eve Lalonde,Jacques Côté,Tatiana G. Kutateladze
摘要
Post-translational modifications (PTMs) of histones provide a fine-tuned mechanism for regulating chromatin structure and dynamics. PTMs can alter direct interactions between histones and DNA and serve as docking sites for protein effectors, or readers, of these PTMs. Binding of the readers recruits or stabilizes various components of the nuclear signaling machinery at specific genomic sites, mediating fundamental DNA-templated processes, including gene transcription and DNA recombination, replication and repair. In this review, we highlight the latest advances in characterizing histone-binding mechanisms and identifying new epigenetic readers and summarize the functional significance of PTM recognition.
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