ArticleNucleic acids research2013
The BAH domain of Rsc2 is a histone H3 binding domain.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
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- PHD-BAH Domain in ASH1L Could Recognize H3K4 Methylation and Regulate the Malignant Behavior of Cholangiocarcinoma.Anti-cancer agents in medicinal chemistry · 2024Article
- Yeast Heterochromatin Only Stably Silences Weak Regulatory Elements by Altering Burst Duration.bioRxiv : the preprint server for biology · 2023Article
- Natural variation in Tiller Number 1 affects its interaction with TIF1 to regulate tillering in rice.Plant biotechnology journal · 2023Article
- Domain Structure of the Dnmt1, Dnmt3a, and Dnmt3b DNA Methyltransferases.Advances in experimental medicine and biology · 2022Article
- Bromodomain-containing subunits BRD1, BRD2, and BRD13 are required for proper functioning of SWI/SNF complexes inPlant communications · 2021Article
- Structure and Function of Chromatin Remodelers.Journal of molecular biology · 2021Review
- A conserved BAH module within mammalian BAHD1 connects H3K27me3 to Polycomb gene silencing.Nucleic acids research · 2021Article
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- Architecture of the chromatin remodeler RSC and insights into its nucleosome engagement.eLife · 2019Article
- Structure of the RSC complex bound to the nucleosome.Science (New York, N.Y.) · 2019Article
- Article
- The BAH domain of BAHD1 is a histone H3K27me3 reader.Protein & cell · 2016Article
- Independent Mechanisms Target SMCHD1 to Trimethylated Histone H3 Lysine 9-Modified Chromatin and the Inactive X Chromosome.Molecular and cellular biology · 2015Article
- Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.Biochemistry · 2015Article
- Structure and function insights into the NuRD chromatin remodeling complex.Cellular and molecular life sciences : CMLS · 2015Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Bromo-adjacent homology (BAH) domains are commonly found in chromatin-associated proteins and fall into two classes; Remodels the Structure of Chromatin (RSC)-like or Sir3-like. Although Sir3-like BAH domains bind nucleosomes, the binding partners of RSC-like BAH domains are currently unknown. The Rsc2 subunit of the RSC chromatin remodeling complex contains an RSC-like BAH domain and, like the Sir3-like BAH domains, we find Rsc2 BAH also interacts with nucleosomes. However, unlike Sir3-like BAH domains, we find that Rsc2 BAH can bind to recombinant purified H3 in vitro, suggesting that the mechanism of nucleosome binding is not conserved. To gain insight into the Rsc2 BAH domain, we determined its crystal structure at 2.4 Å resolution. We find that it differs substantially from Sir3-like BAH domains and lacks the motifs in these domains known to be critical for making contacts with histones. We then go on to identify a novel motif in Rsc2 BAH that is critical for efficient H3 binding in vitro and show that mutation of this motif results in defective Rsc2 function in vivo. Moreover, we find this interaction is conserved across Rsc2-related proteins. These data uncover a binding target of the Rsc2 family of BAH domains and identify a novel motif that mediates this interaction.
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