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- W2895877323 abstract "The eukaryotic genome is packaged into the cell nucleus in the form of chromatin, a complex of genomic DNA and histone proteins. Chromatin structure regulation is critical for all DNA templated processes and involves, among many things, extensive post-translational modification of the histone proteins. These modifications can be “read out” by histone binding subdomains known as histone reader domains. A large number of reader domains have been identified and found to selectively recognize an array of histone post-translational modifications in order to target, retain, or regulate chromatin-modifying and remodeling complexes at their substrates. Interestingly, an increasing number of these histone reader domains are being identified as also harboring nucleic acid binding activity. In this review, we present a summary of the histone reader domains currently known to bind nucleic acids, with a focus on the molecular mechanisms of binding and the interplay between DNA and histone recognition. Additionally, we highlight the functional implications of nucleic acid binding in chromatin association and regulation. We propose that nucleic acid binding is as functionally important as histone binding, and that a significant portion of the as yet untested reader domains will emerge to have nucleic acid binding capabilities." @default.
- W2895877323 created "2018-10-26" @default.
- W2895877323 creator A5030080062 @default.
- W2895877323 creator A5053552465 @default.
- W2895877323 creator A5067188352 @default.
- W2895877323 date "2018-10-12" @default.
- W2895877323 modified "2023-09-29" @default.
- W2895877323 title "Reading More than Histones: The Prevalence of Nucleic Acid Binding among Reader Domains" @default.
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