ArticlePlant physiology2004
A second protein L-isoaspartyl methyltransferase gene in Arabidopsis produces two transcripts whose products are sequestered in the nucleus.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 56 citations in OpenAlex.
- Natural variation in the ZmPIMT1 promoter enhances seed aging tolerance by regulating PABP2 repair in maize.The Plant cell · 2025Article
- Integrative Physiology, Transcriptome, and Metabolome Analysis Reveals Pathways and the Key GeneJournal of agricultural and food chemistry · 2025Article
- Raffinose family oligosaccharides (RFOs): role in seed vigor and longevity.Bioscience reports · 2022Review
- The Arabidopsis TRM61/TRM6 complex is a bona fide tRNA N1-methyladenosine methyltransferase.Journal of experimental botany · 2020Article
- Article
- l-Isoaspartyl Methyltransferase Deficiency in Zebrafish Leads to Impaired Calcium Signaling in the Brain.Frontiers in genetics · 2020Article
- Combined QTL mapping, physiological and transcriptomic analyses to identify candidate genes involved in Brassica napus seed aging.Molecular genetics and genomics : MGG · 2018Article
- Genetic Modification for Improving Seed Vigor Is Transitioning from Model Plants to Crop Plants.Frontiers in plant science · 2017Article
- Protein repair L-isoaspartyl methyltransferase 1 (PIMT1) in rice improves seed longevity by preserving embryo vigor and viability.Plant molecular biology · 2015Article
- A subtle alternative splicing event gives rise to a widely expressed human RNase k isoform.PloS one · 2014Article
- Thermal-stable proteins of fruit of long-living Sacred LotusTropical plant biology · 2013Article
- 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.Plant physiology · 2013Article
- Uses of phage display in agriculture: a review of food-related protein-protein interactions discovered by biopanning over diverse baits.Computational and mathematical methods in medicine · 2013Review
- Substrates of the Arabidopsis thaliana protein isoaspartyl methyltransferase 1 identified using phage display and biopanning.The Journal of biological chemistry · 2010Article
- Quantitative trait loci associated with longevity of lettuce seeds under conventional and controlled deterioration storage conditions.Journal of experimental botany · 2010Article
- Article
- Protein repair L-isoaspartyl methyltransferase 1 is involved in both seed longevity and germination vigor in Arabidopsis.The Plant cell · 2008Article
- Proteome-wide characterization of seed aging in Arabidopsis: a comparison between artificial and natural aging protocols.Plant physiology · 2008Article
- Assessing the fraction of short-distance tandem splice sites under purifying selection.RNA (New York, N.Y.) · 2008Article
- Arabidopsis Protein Repair L-Isoaspartyl Methyltransferases: Predominant Activities at Lethal Temperatures.Physiologia plantarum · 2006Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The spontaneous and deleterious conversion of l-asparaginyl and l-aspartyl protein residues to l-iso-Asp or d-Asp occurs as proteins age and is accelerated under stressful conditions. Arabidopsis (Arabidopsis L. Heynh.) contains two genes (At3g48330 and At5g50240) encoding protein-l-isoaspartate methyltransferase (EC 2.1.1.77; PIMT), an enzyme capable of correcting this damage. The gene located on chromosome 5 (PIMT2) produces two proteins differing by three amino acids through alternative 3' splice site selection in the first intron. Recombinant protein from both splicing variants has PIMT activity. Subcellular localization using cell fractionation followed by immunoblot detection, as well as confocal visualization of PIMT:GFP fusions, demonstrated that PIMT1 is cytosolic while a canonical nuclear localization signal, present in PIMT2psi and the shorter PIMT2omega, is functional. Multiplex reverse transcription-PCR was used to establish PIMT1 and PIMT2 transcript presence and abundance, relative to beta-TUBULIN, in various tissues and under a variety of stresses imposed on seeds and seedlings. PIMT1 transcript is constitutively present but can increase, along with PIMT2, in developing seeds presumably in response to increasing endogenous abscisic acid (ABA). Transcript from PIMT2 also increases in establishing seedlings due to exogenous ABA and applied stress presumably through an ABA-dependent pathway. Furthermore, cleaved amplified polymorphic sequences from PIMT2 amplicons determined that ABA preferentially enhances the production of PIMT2omega transcript in leaves and possibly in tissues other than germinating seeds.
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