
Faculty, Staff and Student Publications
Publication Date
1-11-2025
Journal
Nucleic Acids Research
Abstract
The INO80 chromatin remodeler is a versatile enzyme capable of several functions, including spacing nucleosomes equal distances apart, precise positioning of nucleosomes based on DNA shape/sequence and exchanging histone dimers. Within INO80, the Arp5 subunit plays a central role in INO80 remodeling, evidenced by its interactions with the histone octamer, nucleosomal and extranucleosomal DNA, and its necessity in linking INO80's ATPase activity to nucleosome movement. We find two distinct regions of Arp5 binding near the acidic pocket of nucleosomes. One region has an arginine anchor that binds nucleosomes and is vital for INO80 mobilizing nucleosomes. The other region has a hydrophobic/acid patch of Leu and Asp that binds free histone H2A-H2B dimers. These two regions have different roles in remodeling nucleosomes as seen both in vitro and in vivo and the hydrophobic/acidic patch of Arp5 is likely needed for displacing DNA from the H2A-H2B surface and dimer exchange by INO80.
Keywords
Chromatin Assembly and Disassembly, Nucleosomes, Histones, Saccharomyces cerevisiae Proteins, Protein Conformation, Saccharomyces cerevisiae, Protein Subunits, Protein Binding, DNA, Models, Molecular
DOI
10.1093/nar/gkae1187
PMID
39676660
PMCID
PMC11754651
PubMedCentral® Posted Date
12-16-2024
PubMedCentral® Full Text Version
Post-print
Published Open-Access
yes
Included in
Bioinformatics Commons, Biomedical Informatics Commons, Genetic Phenomena Commons, Medical Genetics Commons, Oncology Commons