The study examined how dual‑purpose hemp (Cannabis sativa) adjusts to different phosphate levels, showing that flower biomass is maintained unless phosphate is completely removed. Integrated physiological measurements and transcriptomic profiling revealed that phosphate is reallocated to flowers via glycolytic bypasses and organic phosphate release, while key regulatory genes followed expected patterns but did not suppress uptake at high phosphate, leading to nitrate depletion that limits growth.
The authors used a bottom‑up thermodynamic modelling framework to investigate how plants decode calcium signals, starting from Ca2+ binding to EF‑hand proteins and extending to higher‑order decoding modules. They identified six universal Ca2+-decoding modules that can explain variations in calcium sensitivity among kinases and provide a theoretical basis for interpreting calcium signal amplitude and frequency in plant cells.
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.
TPS Proteins coordinate plant growth with sugar availability via the SnRK1 Kinase
Authors: Reis-Barata, D., Confraria, A., Margalha, L., Peixoto, B., Lopes, F. L., Belda-Palazon, B., Jurke, B., Arrivault, S., Shukla, V., Feil, R., Licausi, F., Kaschani, F., Kaiser, M., Caldana, C., Stitt, M., Lunn, J. E., Baena-Gonzalez, E.
The study identifies catalytically inactive trehalose‑6‑phosphate synthase proteins TPS5/6/7 as key mediators linking T6P signaling to inhibition of SnRK1 activity, thereby promoting growth in Arabidopsis thaliana. Loss of TPS5/6/7 causes root growth defects and a metabolic profile indicative of T6P insensitivity, which can be rescued by SnRK1 knock‑down, and T6P stimulates a dose‑dependent interaction between TPS proteins and SnRK1.