Data Sheet 1_Structural and functional perspectives on DEAD-box RNA helicases in the rubber tree cold stress response.zip

Their defining architectural feature is a conserved helicase core comprising two tandem RecA-like domains that couples ATP hydrolysis to duplex unwinding and ribonucleoprotein remodeling. Structural investigations have historically focused on human and yeast model systems, but recent methodological advances, particularly cryo-electron microscopy and deep learning-based structure prediction, have broadened the structural coverage of the DDX family, including full-length constructs and their incorporation into multiprotein assemblies.

In plants, DDX helicases remain far less characterized despite their essential functions in development and stress adaptation. This review integrates structural biology insights with recent multi-omics datasets from cold-stressed rubber tree (Hevea brasiliensis), a tropical crop highly susceptible to chilling injury. Quantitative profiling has identified nine differentially abundant DDX proteins under cold stress, among which DDX39B shows the most pronounced response.