ArticleThe Journal of biological chemistry2010
Substrates of the Arabidopsis thaliana protein isoaspartyl methyltransferase 1 identified using phage display and biopanning.
Article in The Journal of biological chemistry, 2010. 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, 42 citations in OpenAlex.
- Transcriptional insights into molecular events occurring during tuber maturation of tigernut (Cyperus esculentus L.).Functional & integrative genomics · 2026Article
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- Late Embryogenesis Abundant Protein-Client Protein Interactions.Plants (Basel, Switzerland) · 2020Review
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- ArabidopsisPlant physiology · 2018Article
- The Gene Encoding Subunit A of the Vacuolar HFrontiers in plant science · 2018Article
- Comparison of Protein N-Homocysteinylation in Rat Plasma under Elevated Homocysteine Using a Specific Chemical Labeling Method.Molecules (Basel, Switzerland) · 2016Article
- Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5.Amino acids · 2016Article
- Protein repair L-isoaspartyl methyltransferase 1 (PIMT1) in rice improves seed longevity by preserving embryo vigor and viability.Plant molecular biology · 2015Article
- Unidirectional movement of cellulose synthase complexes in Arabidopsis seed coat epidermal cells deposit cellulose involved in mucilage extrusion, adherence, and ray formation.Plant physiology · 2015Article
- Synthesis and characterization ofJournal of sulphur chemistry · 2015Article
- Identification and characterization of a novel evolutionarily conserved lysine-specific methyltransferase targeting eukaryotic translation elongation factor 2 (eEF2).The Journal of biological chemistry · 2014Article
- Detection and quantitation of succinimide in intact protein via hydrazine trapping and chemical derivatization.Journal of pharmaceutical sciences · 2014Article
- Discovery of a chemical modification by citric acid in a recombinant monoclonal antibody.Analytical chemistry · 2014Article
- A protocol for phage display and affinity selection using recombinant protein baits.Journal of visualized experiments : JoVE · 2014Article
- An Arabidopsis ATP-dependent, DEAD-box RNA helicase loses activity upon IsoAsp formation but is restored by PROTEIN ISOASPARTYL METHYLTRANSFERASE.The Plant cell · 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
- Article
- Uses of phage display in agriculture: sequence analysis and comparative modeling of late embryogenesis abundant client proteins suggest protein-nucleic acid binding functionality.Computational and mathematical methods in medicine · 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
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Authors and funding
15 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The role of protein isoaspartyl methyltransferase (PIMT) in repairing a wide assortment of damaged proteins in a host of organisms has been inferred from the affinity of the enzyme for isoaspartyl residues in a plethora of amino acid contexts. The identification of PIMT target proteins in plant seeds, where the enzyme is highly active and proteome long-lived, has been hindered by large amounts of isoaspartate-containing storage proteins. Mature seed phage display libraries circumvented this problem. Inclusion of the PIMT co-substrate, S-adenosylmethionine (AdoMet), during panning permitted PIMT to retain aged phage in greater numbers than controls lacking co-substrate or when PIMT protein binding was poisoned with S-adenosyl homocysteine. After four rounds, phage titer plateaued in AdoMet-containing pans, whereas titer declined in both controls. This strategy identified 17 in-frame PIMT target proteins, including a cupin-family protein similar to those identified previously using on-blot methylation. All recovered phage had at least one susceptible Asp or Asn residue. Five targets were recovered independently. Two in-frame targets were produced in Escherichia coli as recombinant proteins and shown by on-blot methylation to acquire isoAsp, becoming a PIMT target. Both gained isoAsp rapidly in solution upon thermal insult. Mutant analysis of plants deficient in any of three in-frame PIMT targets resulted in demonstrable phenotypes. An over-representation of clones encoding proteins involved in protein production suggests that the translational apparatus comprises a subgroup for which PIMT-mediated repair is vital for orthodox seed longevity. Impaired PIMT activity would hinder protein function in these targets, possibly resulting in poor seed performance.
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