ArticleThe Plant cell2013
An Arabidopsis ATP-dependent, DEAD-box RNA helicase loses activity upon IsoAsp formation but is restored by PROTEIN ISOASPARTYL METHYLTRANSFERASE.
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- 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
- Multi-omics Analysis Sheds Light on the Extracellular Role of PCMT1.Journal of proteome research · 2025Article
- An RNA helicase coordinates with iron signal regulators to alleviate chilling stress in Arabidopsis.Nature communications · 2025Article
- Single-nucleus RNA and ATAC sequencing analyses provide molecular insights into early pod development of peanut fruit.Plant communications · 2024Article
- The nuclear GUCT domain-containing DEAD-box RNA helicases govern gametophytic and sporophytic development in Physcomitrium patens.Plant molecular biology · 2021Article
- MicroRNAs expression dynamics reveal post-transcriptional mechanisms regulating seed development in Phaseolus vulgaris L.Horticulture research · 2021Article
- Genome-wide identification, characterisation and expression profile analysis of DEAD-box family genes in sweet potato wild ancestor Ipomoea trifida under abiotic stresses.Genes & genomics · 2020Article
- Article
- Overexpression of a Brix Domain-Containing Ribosome Biogenesis Factor ARPF2 and its Interactor ARRS1 Causes Morphological Changes and Lifespan Extension inFrontiers in plant science · 2018Article
- Function of Plant DExD/H-Box RNA Helicases Associated with Ribosomal RNA Biogenesis.Frontiers in plant science · 2018Review
- A Cold-Inducible DEAD-Box RNA Helicase from Arabidopsis thaliana Regulates Plant Growth and Development under Low Temperature.PloS one · 2016Article
- Posttranslational Protein Modifications in Plant Metabolism.Plant physiology · 2015Article
- Regulation of mRNA translation controls seed germination and is critical for seedling vigor.Frontiers in plant science · 2015Article
- Non-repair pathways for minimizing protein isoaspartyl damage in the yeast Saccharomyces cerevisiae.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
Abstract
Orthodox seeds are capable of withstanding severe dehydration. However, in the dehydrated state, Asn and Asp residues in proteins can convert to succinimide residues that can further react to predominantly form isomerized isoAsp residues upon rehydration (imbibition). IsoAsp residues can impair protein function and can render seeds nonviable, but PROTEIN ISOASPARTYL METHYLTRANSFERASE (PIMT) can initiate isoAsp conversion to Asp residues. The proteins necessary for translation upon imbibition in orthodox seeds may be particularly important to maintain in an active state. One such protein is the large, multidomain protein, Arabidopsis thaliana PLANT RNA HELICASE75 (PRH75), a DEAD-box helicase known to be susceptible to isoAsp residue accumulation. However, the consequences of such isomerization on PRH75 catalysis and for the plant are unknown. Here, it is demonstrated that PRH75 is necessary for successful seed development. It acquires isoAsp rapidly during heat stress, which eliminates RNA unwinding (but not rewinding) competence. The repair by PIMT is able to restore PRH75's complex biochemical activity provided isoAsp formation has not led to subsequent, destabilizing conformational alterations. For PRH75, an important enzymatic activity associated with translation would be eliminated unless rapidly repaired by PIMT prior to additional, deleterious conformational changes that would compromise seed vitality and germination.
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Registered trials
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.