Plant BCL- DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability

• 成果类型: Article
• 署名作者: Candela-Ferre, Joan; Perez-Alemany, Jaime; Diego-Martin, Borja; Pandey, Vijaya; Wohlschlegel, James; Lozano-Juste, Jorge; Gallego-Bartolome, Javier
• 署名单位: Consejo Superior de Investigaciones Cientificas (CSIC); Universitat Politecnica de Valencia; CSIC-UPV - Instituto de Biologia Molecular y Celular de Plantas (IBMCP); University of California System; University of California Los Angeles; University of California Los Angeles Medical Center; David Geffen School of Medicine at UCLA
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-11082
• DOI: 10.1073/pnas.2413346122
• 发表日期: 2025-01-15
• 关键词: actin-related proteins; gene-expression; chromatin; binds

摘要

The SWItch/Sucrose Non- Fermenting (SWI/SNF) complexes are evolutionarily con-served, ATP- dependent chromatin remodelers crucial for multiple nuclear functions in eukaryotes. Recently, plant BCL- DOMAIN HOMOLOG (BDH) proteins were identified as shared subunits of all plant SWI/SNF complexes, significantly impacting chromatin accessibility and various developmental processes in Arabidopsis. In this study, we performed a comprehensive characterization of bdh mutants, revealing the role of BDH in hypocotyl cell elongation. Through detailed analysis of BDH domains, we identified a plant- specific N- terminal domain that facilitates the interaction between BDH and the rest of the complex. Additionally, we uncovered the critical role of the BDH beta- hairpin domain, which is phylogenetically related to mammalian BCL7 SWI/SNF subunits. While phylogenetic analyses did not identify BDH/BCL7 orthologs in fungi, structure prediction modeling demonstrated strong similarities between the SWI/SNF catalytic modules of plants, animals, and fungi and revealed the yeast Rtt102 pro-tein as a structural homolog of BDH and BCL7. This finding is supported by the ability of Rtt102 to interact with the Arabidopsis catalytic module subunit ARP7 and partially rescue the bdh mutant phenotypes. Further experiments revealed that BDH promotes the stability of the ARP4- ARP7 heterodimer, leading to the partial destabilization of ARP4 in the SWI/SNF complexes. In summary, our study unveils the molecular function of BDH proteins in plant SWI/SNF complexes and suggests that beta- hairpin- containing proteins are evolutionarily conserved subunits crucial for ARP heterodimer stability and SWI/SNF activity across eukaryotes.