| Literature DB >> 23211769 |
Catherine A Musselman1, Marie-Eve Lalonde, Jacques Côté, Tatiana G Kutateladze.
Abstract
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.Entities:
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Year: 2012 PMID: 23211769 PMCID: PMC3645987 DOI: 10.1038/nsmb.2436
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369