bims-plasge 2025-07-27 papers

Issue of 2025–07–27
two papers selected by
Vera S. Bogdanova, ИЦиГ СО РАН

Plant Mol Biol. 2025 Jul 23. 115(4): 89

Genetic and molecular approaches for Fusarium wilt resistance in garden pea: advances and future outlook.

Neha Verma, Saurabh Yadav, Neha Rana, Rishabh Maheshwari, Manpreet Kaur, Priyanka Kumari, Parteek Kumar, Rajinder Kumar Dhall, Hira Singh, Priti Sharma, Parveen Chunneja.

Garden pea is an important leguminous crop valued for its protein-rich food source for human nutrition and enhancing agricultural sustainability by fixing nitrogen biologically. However, its cultivation faces significant challenges from pests, diseases, and environmental stresses. Among these, Fusarium wilt (FW) caused by pathogen Fusarium oxysporum f. sp. pisi poses a severe threat, resulting in substantial yield losses globally. Four pathogenic races (1, 2, 5, and 6) of this fungus have been primarily identified, and its broad host range further complicates effective management. Traditional control methods including cultural practices, physical control, biological interventions, and chemical treatments have shown limited efficacy. Consequently, host-plant resistance has emerged as a sustainable and practical solution for managing FW. In this review, the advancements in genetics with modern molecular techniques such as SNP genotyping, QTL mapping, and marker-assisted selection for the development of FW resistant pea varieties were highlighted. Furthermore, we also discussed the omics techniques viz., transcriptomics, metabolomics and proteomics and innovative breeding techniques like CRISPR-mediated genome editing, speed breeding, and genomic selection for revolutionize FW resistance breeding programs in pea. Therefore, this review focuses on integrating cutting-edge molecular techniques with omics approaches to unravel Fusarium wilt defense mechanisms in garden pea, aiming to accelerate genetic gains and develop superior disease-resistant varieties for improved productivity and quality.

Keywords: Fusarium wilt; Genetics; Host plant reaction; Molecular makers; Omics, genome editing ; Speed breeding

DOI: https://doi.org/10.1007/s11103-025-01624-3

J Exp Bot. 2025 Jul 21. pii: eraf329. [Epub ahead of print]

Lon1 Protease Controls PentatricoPeptide-Repeat (PPR)-Mediated RNA Processing in Arabidopsis Mitochondria.

Fengoula Avgeri, Dikran Tsitsekian, Gerasimos Daras, Dimitris Templalexis, Martina Samiotaki, Stamatis Rigas.

Selective proteolysis maintains cellular homeostasis by preventing the accumulation of unfolded or misfolded proteins, which can form deleterious aggregates. Lon is a highly conserved AAA+ (ATPases Associated with diverse cellular Activities) protease in bacteria and eukaryotic organelles, essential for protein quality control. However, the mechanisms of Lon-mediated protein substrate recognition and degradation remain unknown in plant mitochondria. Here, we identify mitochondrial substrates of Arabidopsis Lon1 protease by using a proteolytically inactive Lon1-trap variant in a lon1 mutant background, which exhibits growth retardation due to mitochondrial dysfunction. The identified substrates participate in key mitochondrial pathways, including energy metabolism, transcription and translation, highlighting Lon1's role in maintaining mitochondrial integrity. Notably, we uncover a set of bona fide Lon1 targets, including enzymes involved in calcium transport, lipoic acid synthesis, heat shock responses and PentatricoPeptide-Repeat (PPR) proteins, which are key regulators of mitochondrial gene expression. Strikingly, PPR proteins are highly overrepresented in the lon1 proteome, correlating with defects in group II intron splicing and RNA editing, particularly in transcripts encoding Complex I subunits, cytochrome c biogenesis factors, Complex IV components and ribosomal proteins. Our findings reveal a novel regulatory role for Lon1 in mitochondrial RNA processing and maturation through selective proteolysis of PPR proteins.

Keywords: Arabidopsis; Lon; PPR proteins; RNA editing; RNA splicing; mitochondria; proteolysis

DOI: https://doi.org/10.1093/jxb/eraf329