ArticleInternational journal of molecular sciences2023
BRM Complex in Arabidopsis Adopts ncBAF-like Composition and Requires BRD Subunits for Assembly and Stability.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 10 citations in OpenAlex.
- Structure and molecular function of the BCL7 proteins.Biochemical Society transactions · 2026Review
- SMARCD1 and Its Functional Relevance in SWI/SNF and Cancer.International journal of molecular sciences · 2026Review
- BAF60/SWP73 subunits define subclasses of SWI/SNF chromatin remodelling complexes in Arabidopsis.The New phytologist · 2025Article
- 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
- Isolation and Identification of Nuclear Protein Complexes Using GFP-Tagged Arabidopsis Lines and IP-MS Approach.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The BRAHMA-associated SWI/SNF chromatin remodeling complex controls Arabidopsis seed quality and physiology.Plant physiology · 2024Article
- Plant BCL-Domain Homologues play a conserved role in SWI/SNF complex stability.bioRxiv : the preprint server for biology · 2024Article
- Characterization of the SWI/SNF complex and nucleosome organization in sorghum.Frontiers in plant science · 2024Article
- Spotlight on Plant Bromodomain Proteins.Biology · 2023Review
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Authors and funding
10 authors at 2 institutions in 1 country.
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Abstract
ATP-dependent SWI/SNF chromatin remodelling complexes are conserved multi-subunit assemblies that control genome activity. Functions of SWI/SNF complexes in plant development and growth have been well established, but the architecture of particular assemblies is unclear. In this study, we elucidate the organization of Arabidopsis SWI/SNF complexes formed around a BRM catalytic subunit, and define the requirement of bromodomain-containing proteins BRD1/2/13 for the formation and stability of the entire complex. Using affinity purification followed by mass spectrometry, we identify a set of BRM-associated subunits and demonstrate that the BRM complexes strongly resemble mammalian non-canonical BAF complexes. Furthermore, we identify BDH1 and 2 proteins as components of the BRM complex and, using mutant analyses, show that BDH1/2 are important for vegetative and generative development, as well as hormonal responses. We further show that BRD1/2/13 represent unique subunits of the BRM complexes, and their depletion severely affects the integrity of the complex, resulting in the formation of residual assemblies. Finally, analyses of BRM complexes after proteasome inhibition revealed the existence of a module consisting of the ATPase, ARP, and BDH proteins, assembled with other subunits in a BRD-dependent manner. Together, our results suggest modular organization of plant SWI/SNF complexes and provide a biochemical explanation for mutant phenotypes.
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