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

• DOI: 10.1073/pnas.2413346122
• Publication Date: 2025-01-17T18:35:51Z
• Authors: Joan Candela-Ferre; Jaime Pérez-Alemany; Borja Diego-Martin; Vijaya Pandey; James Wohlschlegel; Jorge Lozano-Juste; Javier Gallego-Ba...

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