ArticlePlant physiology2013
PROTEIN L-ISOASPARTYL METHYLTRANSFERASE2 is differentially expressed in chickpea and enhances seed vigor and longevity by reducing abnormal isoaspartyl accumulation predominantly in seed nuclear proteins.
Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
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Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.
- Seed Longevity in Legumes: Deeper Insights Into Mechanisms and Molecular Perspectives.Frontiers in plant science · 2022Pooled it
- Rice PROTEIN L-ISOASPARTYL METHYLTRANSFERASES provides tolerance against sheath blight disease and repairs ALDH and PBZ1.Nature communications · 2026Article
- Molecular timekeepers: the curious alliance of redox, repair, and protective proteins in preserving seed longevity.Crop health · 2026Review
- Natural variation in the ZmPIMT1 promoter enhances seed aging tolerance by regulating PABP2 repair in maize.The Plant cell · 2025Article
- Deciphering Seed Deterioration: Molecular Insights and Priming Strategies for Revitalizing Aged Seeds.Plants (Basel, Switzerland) · 2025Review
- Unraveling the Mechanistic Basis for Control of Seed Longevity.Plants (Basel, Switzerland) · 2025Review
- Comparative regulatory network of transcripts behind radicle emergence and seedling stage of maize (Heliyon · 2024Article
- Integrated multispectral imaging, germination phenotype, and transcriptomic analysis provide insights into seed vigor responsive mechanisms in quinoa under artificial accelerated aging.Frontiers in plant science · 2024Article
- The Arabidopsis F-box protein SKP1-INTERACTING PARTNER 31 modulates seed maturation and seed vigor by targeting JASMONATE ZIM DOMAIN proteins independently of jasmonic acid-isoleucine.The Plant cell · 2023Article
- Raffinose family oligosaccharides (RFOs): role in seed vigor and longevity.Bioscience reports · 2022Review
- AtZAT4, a CPlants (Basel, Switzerland) · 2022Article
- Nitric oxide-an antidote to seed aging modifiesFrontiers in plant science · 2022Article
- Comparative Proteomics at the Critical Node of Vigor Loss in Wheat Seeds Differing in Storability.Frontiers in plant science · 2021Article
- Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge.Insects · 2020Article
- Article
- Combined QTL mapping, physiological and transcriptomic analyses to identify candidate genes involved in Brassica napus seed aging.Molecular genetics and genomics : MGG · 2018Article
- Arabidopsis SKP1-like protein13 (ASK13) positively regulates seed germination and seedling growth under abiotic stress.Journal of experimental botany · 2018Article
- RNA-Seq using bulked recombinant inbred line populations uncovers the importance of brassinosteroid for seed longevity after priming treatments.Scientific reports · 2017Article
- Genetic Modification for Improving Seed Vigor Is Transitioning from Model Plants to Crop Plants.Frontiers in plant science · 2017Article
- Differentially expressed galactinol synthase(s) in chickpea are implicated in seed vigor and longevity by limiting the age induced ROS accumulation.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PROTEIN l-ISOASPARTYL METHYLTRANSFERASE (PIMT) is a widely distributed protein-repairing enzyme that catalyzes the conversion of abnormal l-isoaspartyl residues in spontaneously damaged proteins to normal aspartyl residues. This enzyme is encoded by two divergent genes (PIMT1 and PIMT2) in plants, unlike many other organisms. While the biological role of PIMT1 has been elucidated, the role and significance of the PIMT2 gene in plants is not well defined. Here, we isolated the PIMT2 gene (CaPIMT2) from chickpea (Cicer arietinum), which exhibits a significant increase in isoaspartyl residues in seed proteins coupled with reduced germination vigor under artificial aging conditions. The CaPIMT2 gene is found to be highly divergent and encodes two possible isoforms (CaPIMT2 and CaPIMT2') differing by two amino acids in the region I catalytic domain through alternative splicing. Unlike CaPIMT1, both isoforms possess a unique 56-amino acid amino terminus and exhibit similar yet distinct enzymatic properties. Expression analysis revealed that CaPIMT2 is differentially regulated by stresses and abscisic acid. Confocal visualization of stably expressed green fluorescent protein-fused PIMT proteins and cell fractionation-immunoblot analysis revealed that apart from the plasma membrane, both CaPIMT2 isoforms localize predominantly in the nucleus, while CaPIMT1 localizes in the cytosol. Remarkably, CaPIMT2 enhances seed vigor and longevity by repairing abnormal isoaspartyl residues predominantly in nuclear proteins upon seed-specific expression in Arabidopsis (Arabidopsis thaliana), while CaPIMT1 enhances seed vigor and longevity by repairing such abnormal proteins mainly in the cytosolic fraction. Together, our data suggest that CaPIMT2 has most likely evolved through gene duplication, followed by subfunctionalization to specialize in repairing the nuclear proteome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.