Reading More than Histones: The Prevalence of Nucleic Acid Binding among Reader Domains. Molecules 2018 Oct 12;23(10)
Date
10/17/2018Pubmed ID
30322003Pubmed Central ID
PMC6222470DOI
10.3390/molecules23102614Scopus ID
2-s2.0-85054890627 (requires institutional sign-in at Scopus site) 36 CitationsAbstract
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.
Author List
Weaver TM, Morrison EA, Musselman CAAuthor
Emma A. Morrison PhD Assistant Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsBinding Sites
DNA
Histones
Humans
Models, Molecular
Prevalence
Protein Binding
Protein Domains
