Evolution of HMA-integrated tandem kinases accompanied by expansion of target pathogens
Authors: Asuke, S., Tagle, A. G., Hyon, G.-S., Koizumi, S., Murakami, T., Horie, A., Niwamoto, D., Katayama, E., Shibata, M., Takahashi, Y., Islam, M. T., Matsuoka, Y., Yamaji, N., Shimizu, M., Terauchi, R., Hisano, H., Sato, K., Tosa, Y.
The study cloned the resistance genes Rmo2 and Rwt7 from barley and wheat, revealing them as orthologous tandem kinase proteins (TKPs) with an N‑terminal heavy metal‑associated (HMA) domain. Domain‑swapping experiments indicated that the HMA domain dictates effector specificity, supporting a model of TKP diversification into paralogs and orthologs that recognize distinct pathogen effectors.
Mutations in the plastid division gene PARC6 and the granule initiation gene BGC1 were combined to generate wheat plants with dramatically enlarged A-type starch granules, some exceeding 50 µm, without affecting plant growth, grain size, or overall starch content. The parc6 bgc1 double mutant was evaluated in both glasshouse and field trials, and the giant granules displayed altered viscosity and pasting temperature, offering novel functional properties for food and industrial applications.
Using ten Phaeodactylum tricornutum mutant strains with graded constitutive Lhcx1 expression, the study links NPQ induction under high light to physiological outcomes (oxidized QA, increased cyclic electron flow) and extensive transcriptomic reprogramming, affecting nearly half the genome. The approach demonstrates that higher NPQ mitigates PSII damage, boosts ATP production for repair, and drives distinct gene regulatory networks, providing a model framework for dissecting photosynthetic and gene expression integration.
The study establishes a tractable system using the large bloom-forming diatom Coscinodiscus granii and its natural oomycete parasite Lagenisma coscinodisci, enabling manual isolation of single host cells and stable co-cultures. High‑quality transcriptomes for both partners were assembled, revealing diverse oomycete effectors and a host transcriptional response involving proteases and exosome pathways, while also profiling the co‑occurring heterotrophic flagellate Pteridomonas sp. This tripartite platform provides a unique marine model for dissecting molecular mechanisms of oomycete‑diatom interactions.
Glycosylated diterpenes associate with early containment of Fusarium culmorum infection across wheat (Triticum aestivum L.) genotypes under field conditions
Authors: Pieczonka, S. A., Dick, F., Bentele, M., Ramgraber, L., Prey, L., Kupczyk, E., Seidl-Schulz, J., Hanemann, A., Noack, P. O., Asam, S., Schmitt-Kopplin, P., Rychlik, M.
The researchers performed a large‑scale field trial with 105 wheat (Triticum aestivum) genotypes inoculated by Fusarium culmorum, combining quantitative deoxynivalenol (DON) profiling and untargeted metabolomics to uncover molecular signatures of infection. Sesquiterpene‑derived metabolites tracked toxin accumulation, whereas glycosylated diterpene conjugates were enriched in low‑DON samples, indicating a potential defensive metabolic pathway.
The study reveals that rice perceives Xanthomonas oryzae pv. oryzae outer membrane vesicles through a rapid calcium signal that triggers plasma‑membrane nanodomain formation and the re‑organisation of defence‑related proteins, establishing an early immune response. Without this Ca2+ signal, OMVs are not recognized and immunity is weakened.
Authors: Baer, M., Zhong, Y., Yu, B., Tian, T., He, X., Gu, L., Huang, X., Gallina, E., Metzen, I. E., Bucher, M., Song, R., Gutjahr, C., SU, Z., Moya, Y., von Wiren, N., Zhang, L., Yuan, L., Shi, Y., Wang, S., Qi, W., Baer, M., Zhao, Z., Li, C., Li, X., Hochholdinger, F., Yu, P.
The study uncovers how arbuscular mycorrhizal (AM) fungi induce lateral root formation in maize by activating ethylene‑responsive transcription factors (ERFs) that regulate pericycle cell division and reshape flavonoid metabolism, lowering inhibitory flavonols. It also shows that the rhizobacterium Massilia collaborates with AM fungi, degrading flavonoids and supplying auxin, thereby creating an integrated ethylene‑flavonoid‑microbe signaling network that can be harnessed to improve nutrient uptake and crop sustainability.
The study generated time‑resolved transcriptomes (0, 6, 24 h post‑inoculation) from grapevine genotypes carrying single, double, or triple resistance loci against Plasmopara viticola and a susceptible control. Multilocus genotypes showed baseline transcriptional differences and distinct, non‑additive co‑expression network rewiring, with specific immune‑layer dynamics and rapid induction of transcription factors in the triple‑locus line. These findings reveal that pyramiding resistance loci alters the timing, connectivity, and layer allocation of immune‑related transcriptional programs.
The study compares the iron-poor oceanic diatom Thalassiosira oceanica with the iron-rich coastal species T. pseudonana to uncover how diatoms adapt to low-iron conditions. Using photo‑physiological measurements, proteomic profiling, and focused ion beam scanning electron microscopy, the researchers show that each species remodels chloroplast compartments and exhibits distinct mitochondrial architectures to maintain chloroplast‑mitochondrial coupling under iron limitation.
CLPC2 plays specific roles in CLP complex-mediated regulation of growth, photosynthesis, embryogenesis and response to growth-promoting microbial compounds
Authors: Leal-Lopez, J., Bahaji, A., De Diego, N., Tarkowski, P., Baroja-Fernandez, E., Munoz, F. J., Almagro, G., Perez, C. E., Bastidas-Parrado, L. A., Loperfido, D., Caporalli, E., Ezquer, I., Lopez-Serrano, L., Ferez-Gomez, A., Coca-Ruiz, V., Pulido, P., Morcillo, R. J. L., Pozueta-Romero, J.
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.