Root-Suppressed Phenotype of Tomato Rs Mutant is Seemingly Related to Expression of Root-Meristem-Specific Sulfotransferases
Authors: Kumari, A., Gupta, P., Santisree, P., Pamei, I., Valluri,, S., Sharma, K., Venkateswara Rao, K., Shukla, S., Nama, S., Sreelakshmi, Y., Sharma, R.
The study characterizes a radiation‑induced root‑suppressed (Rs) mutant in tomato that displays dwarfism and pleiotropic defects in leaves, flowers, and fruits. Metabolite profiling and rescue with H2S donors implicate disrupted sulfur metabolism, and whole‑genome sequencing identifies promoter mutations in two root‑meristem‑specific sulfotransferase genes as likely contributors to the root phenotype.
The study introduced charge-altering mutations into the N‑terminal region of Lhcb2 in Arabidopsis thaliana lacking native Lhcb2 to assess how intrinsic charge affects LHCII phosphorylation, state‑transition efficiency, and PSI‑LHCII complex formation. The R2E mutation drastically reduced Lhcb1/2 phosphorylation, impaired state transitions, and prevented PSI‑LHCII assembly, whereas the Q9E mutation had no measurable impact, and neither mutation altered thylakoid ultrastructure. Residual state transitions in the R2E line suggest that other Stn7 substrates can partially compensate for the loss of Lhcb2 phosphorylation.
An ancient alkalinization factor informs Arabidopsis root development
Authors: Xhelilaj, K., von Arx, M., Biermann, D., Parvanov, A., Faiss, N., Monte, I., Klingelhuber, F., Zipfel, C., Timmermans, M., Oecking, C., Gronnier, J.
The study identifies members of the REMORIN protein family as inhibitors of plasma membrane H⁺‑ATPases, leading to extracellular pH alkalinization that modulates cell surface processes such as steroid hormone signaling and coordinates root developmental transitions in Arabidopsis thaliana. This inhibition represents an ancient mechanism predating root evolution, suggesting that extracellular pH patterning has shaped plant morphogenesis.
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 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 generated deep proteome and phosphoproteome datasets from guard cell‑enriched tissue to examine how phosphorylation regulates stomatal movements. Comparative analysis revealed increased phosphorylation of endomembrane trafficking and vacuolar proteins in closed stomata, supporting a role for phospho‑regulated trafficking in stomatal dynamics.
EPP1 is an ancestral component of the plant Common SymbiosisPathway
Authors: Rich, M. K., Vernie, T., Tiwari, M., Chauderon, L., Causse, J., Pellen, T., Boussaroque, A., Bianconi, M. E., Vandenbussche, M., Chambrier, P., Le Ru, A., Castel, B., Nagalla, S., Cullimore, J., Keller, J., Valdes-Lopez, O., Mbengue, M., Ane, J.-M., Delaux, P.-M.
The study identifies EPP1 as a fourth, conserved component of the ancestral common symbiosis pathway required for intracellular plant–microbe interactions, showing that its loss impairs arbuscular mycorrhizal colonization across diverse plant clades. EPP1 is phosphorylated by the plasma‑membrane receptor SYRMK, and this modification is essential for downstream activation of the nuclear kinase CCaMK, positioning EPP1 upstream in the signaling cascade.
The study demonstrates that ABI5‑Binding Proteins (AFPs) interact with multiple components of the core ABA signaling pathway and serve as substrates for SnRK2 kinases and PP2C phosphatases, linking them to MAP kinases and 14‑3‑3 proteins. Phosphorylation of AFP2, promoted by ABA, stabilizes the protein and influences its subcellular localization, thereby modulating its ability to inhibit ABA responses during seed germination.
The study profiled root transcriptomes of Arabidopsis wild type and etr1 gain-of-function (etr1-3) and loss-of-function (etr1-7) mutants under ethylene or ACC treatment, identifying 4,522 ethylene‑responsive transcripts, including 553 that depend on ETR1 activity. ETR1‑dependent genes encompassed ethylene biosynthesis enzymes (ACO2, ACO3) and transcription factors, whose expression was further examined in an ein3eil1 background, revealing that both ETR1 and EIN3/EIL1 pathways regulate parts of the network controlling root hair proliferation and lateral root formation.
The study identifies the RNA‑binding protein AtG3BP1 as a phosphorylation target of MAPKs MPK3, MPK4, and MPK6 at Ser257 in Arabidopsis thaliana and shows that this modification promotes susceptibility to bacterial pathogens, suppresses ROS accumulation and salicylic acid biosynthesis, and maintains stomatal opening. Phospho‑mimic and phospho‑dead mutants reveal that phosphorylation stabilizes AtG3BP1 by preventing proteasomal degradation, highlighting a novel post‑translational control layer in plant immunity.