Rice PROTEIN L-ISOASPARTYL METHYLTRANSFERASES provides tolerance against sheath blight disease and repairs ALDH and PBZ1

dc.contributor.authorGautam, Shikha
dc.contributor.authorKamble, Nitin Uttam
dc.contributor.authorAchary, Rakesh Kumar
dc.contributor.authorChandan, Ravindra Kumar
dc.contributor.authorVarshney, Vishal
dc.contributor.authorHazra, Abhijit
dc.contributor.authorLaha, Saroj
dc.contributor.authorMahawar, Shivangi
dc.contributor.authorMehandiratta, Sohela
dc.contributor.authorSingh, Sarvanand
dc.contributor.authorJha, Gopaljee
dc.contributor.authorMajee, Manoj
dc.date.accessioned2026-07-28T09:16:20Z
dc.date.issued2026
dc.descriptionAccepted date: 01 July 2026
dc.description.abstractProtein L-isoaspartyl methyltransferase (PIMT) regulates key seed traits and abiotic stress tolerance in plants by repairing isoaspartyl (isoAsp) damaged proteins. However, whether PIMT-mediated repair is induced and is required during biotic stress tolerance remains unknown. Using rice lines with OsPIMT overexpression, RNAi-mediated suppression, and genome editing, we show that PIMT enhances tolerance to sheath blight (ShB) caused by Rhizoctonia solani. OsPIMT restricts fungal penetration and colonization of rice sheaths. Co-immunoprecipitation coupled with LC-MS/MS identify various proteins including antioxidant proteins, aldehyde dehydrogenases (ALDH) and pathogenesis-related protein 10 (PBZ1), that undergo isoAsp modification during R. solani infection and interact with PIMT. We show that OsALDH and OsPBZ1 exhibit intrinsic antifungal activity against R. solani, but isoAsp modification impairs their activity, making PIMT mediated repair important. Further, OsALDH enhances tolerance to R. solani by inhibiting lipid peroxidation and ROS homeostasis in rice and fungus. Overall, our study reveals that PIMT enhances ShB tolerance through the repair of isoAsp-damaged proteins important for disease tolerance.
dc.description.sponsorshipThe authors thank the BRIC-NIPGR metabolome facility and proteomic facility [DBT grant (no. BT/INF/22/SP28268/2018)], confocal microscopy facility, radioisotope facility, and central instrumentation facility. The authors thank the technicians Ms. Umamaheswari Rajamani and Shri Naga Vara Prasad G of the NIPGR proteomic facility for assisting with MS/MS analysis and data submission. G.J. acknowledges SR-NBACD award (HRD-20/3/2024-HRD-DBT), Swarna Jayanti Fellowship (SB/SJF/2020-21/01; ANRF (SERB)-funded), CRG grant (CRG/2022/004092, ANRF (SERB)-funded), and BRIC-NIPGR core research grant. N.U.K. acknowledges the Indian Institute of Science Education and Research, Thiruvananthapuram, for the core research grant. R.K.C. acknowledges financial support from the DBT-RA program in Biotechnology and Life Sciences. The authors are thankful to the DBT-eLibrary Consortium (DeLCON) for providing access to e-resources. This work was supported by a grant from the Department of Biotechnology, Government of India (BT/NIPGR/Flagship-prog/2018-19) and a core grant to M.M. from the BRIC-National Institute of Plant Genome Research. All authors gratefully thank the Council of Scientific and Industrial Research, University Grant Commission, Department of Biotechnology, Government of India, and BRIC-National Institute of Plant Genome Research for research fellowships.
dc.identifier.citationNature Communications, (In Press)
dc.identifier.issn2041-1723
dc.identifier.otherhttps://doi.org/10.1038/s41467-026-75618-0
dc.identifier.urihttps://www.nature.com/articles/s41467-026-75618-0
dc.identifier.urihttps://ndkr-library.nipgr.ac.in/handle/123456789/1836
dc.language.isoen_US
dc.publisherNature Publishing Group
dc.subjectRice
dc.subjectPROTEIN L-ISOASPARTYL METHYLTRANSFERASES
dc.subjectsheath blight disease
dc.subjectALDH and PBZ1
dc.titleRice PROTEIN L-ISOASPARTYL METHYLTRANSFERASES provides tolerance against sheath blight disease and repairs ALDH and PBZ1
dc.typeArticle

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