The study demonstrates that the plastid chaperone CLPC2, but not its paralogue CLPC1, is essential for Arabidopsis responsiveness to microbial volatile compounds and for normal seed and seedling development. Loss of CLPC2 alters the chloroplast proteome, affecting proteins linked to growth, photosynthesis, and embryogenesis, while overexpression of CLPC2 mimics CLPC1 deficiency, highlighting distinct functional roles within the CLP protease complex.

The authors compiled and standardized published data on Rubisco dark inhibition for 157 flowering plant species, categorizing them into four inhibition levels and analyzing phylogenetic trends. Their meta‑analysis reveals a complex, uneven distribution of inhibition across taxa, suggesting underlying chloroplast microenvironment drivers and providing a new resource for future photosynthesis improvement efforts.

The study reveals that brassinosteroids activate phosphoenolpyruvate carboxykinase (PCK) by promoting dephosphorylation of conserved Ser-62 and Thr-66 residues, a process antagonized by the GSK3-like kinase BIN2. BR‑deficient Arabidopsis mutants exhibit reduced PCK activity, while phospho‑blocking mutations confer BR‑independent activation and enhanced seedling growth, and similar regulatory mechanisms are observed in maize and sorghum leaves.

The study investigated how brassinosteroids and their inhibitor affect G-fiber development and the twining habit in common bean by applying hormones, then analyzing anatomical, biochemical, and transcriptomic changes. Brassinosteroid treatment produced elongated internodes with thin-walled G‑fibers, while inhibition yielded short internodes with thick G‑fibers, both linked to differential expression of XTH genes and xyloglucan remodeling in the G‑layer.

The study quantitatively measures binding kinetics of four Arabidopsis thaliana brassinosteroid receptors with fifteen BRs, identifying chemical features required for high‑affinity binding and co‑receptor recognition. Structural analysis of BR‑bound receptor ectodomains combined with extensive in vitro and in vivo mutagenesis reveals a highly plastic hormone‑binding pocket, and functional assays with structure‑based agonists and antagonists show that receptor‑co‑receptor complexes can accommodate chemically diverse BRs, adding a new regulatory layer to BR signaling.