ArticleThe Journal of biological chemistry2015
Assembly of the Arp5 (Actin-related Protein) Subunit Involved in Distinct INO80 Chromatin Remodeling Activities.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- The Prion-Like Properties of the INO80 Chromatin Remodeler Regulate Metabolic Gene Expression.bioRxiv : the preprint server for biology · 2026Article
- The Ies6 subunit is essential for INO80-mediated nucleosome organization.Scientific reports · 2026Article
- Conformational switching of Arp5 subunit regulates INO80 chromatin remodeling.Nucleic acids research · 2025Article
- Chromatin sensing: integration of environmental signals to reprogram plant development through chromatin regulators.Journal of experimental botany · 2024Review
- Conformational switching of Arp5 subunit differentially regulates INO80 chromatin remodeling.bioRxiv : the preprint server for biology · 2024Article
- New insights into the mechanism and DNA-sequence specificity of INO80 chromatin remodeling.Research square · 2023Article
- Envisioning a role for nuclear actin in prophase I spermatocytes.Frontiers in cell and developmental biology · 2023Review
- A hexasome is the preferred substrate for the INO80 chromatin remodeling complex, allowing versatility of function.Molecular cell · 2022Article
- Article
- Nuclear Actin Dynamics in Gene Expression, DNA Repair, and Cancer.Results and problems in cell differentiation · 2022Article
- The chromatin remodeler Ino80 mediates RNAPII pausing site determination.Genome biology · 2021Article
- Sophisticated Conversations between Chromatin and Chromatin Remodelers, and Dissonances in Cancer.International journal of molecular sciences · 2021Review
- INO80 and SWR1 complexes: the non-identical twins of chromatin remodelling.Current opinion in structural biology · 2020Review
- Molecular basis for chromatin assembly and modification by multiprotein complexes.Protein science : a publication of the Protein Society · 2019Review
- Structure and dynamics of the yeast SWR1-nucleosome complex.Science (New York, N.Y.) · 2018Article
- The Arp8 and Arp4 module acts as a DNA sensor controlling INO80 chromatin remodeling.Nature communications · 2018Article
- Article
- The INO80 chromatin remodeler sustains metabolic stability by promoting TOR signaling and regulating histone acetylation.PLoS genetics · 2018Article
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- Genome maintenance functions of the INO80 chromatin remodeller.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
ATP-dependent chromatin remodeling, which repositions and restructures nucleosomes, is essential to all DNA-templated processes. The INO80 chromatin remodeling complex is an evolutionarily conserved complex involved in diverse cellular processes, including transcription, DNA repair, and replication. The functional diversity of the INO80 complex can, in part, be attributed to specialized activities of distinct subunits that compose the complex. Furthermore, structural analyses have identified biochemically discrete subunit modules that assemble along the Ino80 ATPase scaffold. Of particular interest is the Saccharomyces cerevisiae Arp5-Ies6 module located proximal to the Ino80 ATPase and the Rvb1-Rvb2 helicase module needed for INO80-mediated in vitro activity. In this study we demonstrate that the previously uncharacterized Ies2 subunit is required for Arp5-Ies6 association with the catalytic components of the INO80 complex. In addition, Arp5-Ies6 module assembly with the INO80 complex is dependent on distinct conserved domains within Arp5, Ies6, and Ino80, including the spacer region within the Ino80 ATPase domain. Arp5-Ies6 interacts with chromatin via assembly with the INO80 complex, as IES2 and INO80 deletion results in loss of Arp5-Ies6 chromatin association. Interestingly, ectopic addition of the wild-type Arp5-Ies6 module stimulates INO80-mediated ATP hydrolysis and nucleosome sliding in vitro. However, the addition of mutant Arp5 lacking unique insertion domains facilitates ATP hydrolysis in the absence of nucleosome sliding. Collectively, these results define the requirements of Arp5-Ies6 assembly, which are needed to couple ATP hydrolysis to productive nucleosome movement.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.