ArticleThe Journal of biological chemistry2013
Subunit Rtt102 controls the conformation of the Arp7/9 heterodimer and its interactions with nucleotide and the catalytic subunit of SWI/SNF remodelers.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Structure and molecular function of the BCL7 proteins.Biochemical Society transactions · 2026Review
- BCL7A's arginine anchor links nucleosome recognition to chromatin remodeling and diffuse large B-cell lymphoma tumor suppression.Protein & cell · 2026Article
- Structural basis for BCL7B-mediated ncBAF-nucleosome engagement.Nucleic acids research · 2026Article
- Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural and functional characterisation and regulatory mechanisms of SWI/SNF and RSC chromatin remodelling complexes in fungi.Mycology · 2025Review
- Plant BCL-Domain Homologues play a conserved role in SWI/SNF complex stability.bioRxiv : the preprint server for biology · 2024Article
- Article
- The RSC (Remodels the Structure of Chromatin) complex of Candida albicans shows compositional divergence with distinct roles in regulating pathogenic traits.PLoS genetics · 2020Article
- The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling.Nature structural & molecular biology · 2018Article
- Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase.Communications biology · 2018Article
- Regulation of DNA Translocation Efficiency within the Chromatin Remodeler RSC/Sth1 Potentiates Nucleosome Sliding and Ejection.Molecular cell · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Chromatin-remodeling complexes are assembled around a catalytic subunit that contains a central ATPase domain and flanking sequences that recruit auxiliary subunits. The catalytic subunits of SWI/SNF remodelers recruit Arp7/9 through a helicase/SANT-associated (HSA) domain N-terminal to the ATPase domain. Arp7/9-containing remodelers also carry the auxiliary subunit Rtt102, but the role of this subunit is poorly understood. Here, we show that Rtt102 binds with nanomolar affinity to the Arp7/9 heterodimer and modulates its conformation and interactions with the ATPase subunit and nucleotide. When bound to Rtt102, Arp7/9 interacts with a shorter segment of the HSA domain. Structural analysis by small-angle x-ray scattering further shows that when bound to Rtt102, the complex of Arp7/9 with the catalytic subunit assumes a more stable compact conformation. We also found that Arp7, Arp9, and Arp7/9 interact very weakly with ATP, but Rtt102 promotes high-affinity ATP binding to a single site in the heterodimer. Collectively, the results establish a function for subunit Rtt102 as a stabilizing factor for the Arp7/9 heterodimer, enhancing its interaction with nucleotide and controlling the conformation of SWI/SNF remodelers in an Arp7/9-dependent manner.
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