Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/1591
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dc.contributor.authorKamble, Nitin Uttam-
dc.contributor.authorGhosh, Shraboni-
dc.contributor.authorPetla, Bhanu Prakash-
dc.contributor.authorAchary, Rakesh Kumar-
dc.contributor.authorGautam, Shikha-
dc.contributor.authorRao, Venkateswara-
dc.contributor.authorSalvi, Prafull-
dc.contributor.authorHazra, Abhijit-
dc.contributor.authorVarshney, Vishal-
dc.contributor.authorMajee, Manoj-
dc.date.accessioned2024-04-19T10:55:48Z-
dc.date.available2024-04-19T10:55:48Z-
dc.date.issued2024-
dc.identifier.citationPlant Journal, 119(1): 413-431en_US
dc.identifier.issn0960-7412-
dc.identifier.issn1365-313X-
dc.identifier.otherhttps://doi.org/10.1111/tpj.16771-
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/10.1111/tpj.16771-
dc.identifier.urihttp://223.31.159.10:8080/jspui/handle/123456789/1591-
dc.descriptionAccepted date: 31 March 2024en_US
dc.description.abstractThe protein-repairing enzyme (PRE) PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) influences seed vigor by repairing isoaspartyl-mediated protein damage in seeds. However, PIMTs function in other seed traits, and the mechanisms by which PIMT affects such seed traits are still poorly understood. Herein, through molecular, biochemical, and genetic studies using overexpression and RNAi lines in Oryza sativa and Arabidopsis thaliana, we demonstrate that PIMT not only affects seed vigor but also affects seed size and weight by modulating enolase (ENO) activity. We have identified ENO2, a glycolytic enzyme, as a PIMT interacting protein through Y2H cDNA library screening, and this interaction was further validated by BiFC and co-immunoprecipitation assay. We show that mutation or suppression of ENO2 expression results in reduced seed vigor, seed size, and weight. We also proved that ENO2 undergoes isoAsp modification that affects its activity in both in vivo and in vitro conditions. Further, using MS/MS analyses, amino acid residues that undergo isoAsp modification in ENO2 were identified. We also demonstrate that PIMT repairs such isoAsp modification in ENO2 protein, protecting its vital cellular functions during seed maturation and storage, and plays a vital role in regulating seed size, weight, and seed vigor. Taken together, our study identified ENO2 as a novel substrate of PIMT, and both ENO2 and PIMT in turn implicate in agronomically important seed traits.en_US
dc.description.sponsorshipWe thank Dr. David Seung (John Innes Centre, Norwich, UK), foradvice. We thank the NIPGR metabolome facility and proteomicfacility [DBT grant (no. BT/INF/22/SP28268/2018)], confocal micros-copy facility and central instrumentation facility. The authors arethankful to DBT-eLibrary Consortium (DeLCON) for providingaccess to e-resources. Model was created using Biorender(BioRender.com). This work was supported by a grant from the Departmentof Biotechnology (BT/HRD/NBA/39/05/2018-19), the Govern-ment of India, and a core grant from the National Instituteof Plant Genome Research. All authors gratefully thank theCouncil of Scientific and Industrial Research, UniversityGrant Commission, Government of India, and NationalInstitute of Plant Genome Research for research fellowships.en_US
dc.language.isoen_USen_US
dc.publisherJohn Wiley & Sonsen_US
dc.subjectArabidopsis thalianaen_US
dc.subjectPIMTen_US
dc.subjectenolaseen_US
dc.subjectriceen_US
dc.subjectseed sizeen_US
dc.subjectseed vigoren_US
dc.titlePROTEIN L-ISOASPARTYL METHYLTRANSFERASE protects enolase dysfunction by repairing isoaspartyl-induced damage and is positively implicated in agronomically important seed traitsen_US
dc.typeArticleen_US
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