ArticlePlant physiology2009
The RNA hydrolysis and the cytokinin binding activities of PR-10 proteins are differently performed by two isoforms of the Pru p 1 peach major allergen and are possibly functionally related.
Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 72 citations in OpenAlex.
- Article
- Worldwide Heterogeneity of Food Allergy: Focus on Peach Allergy in Southern Italy.Journal of clinical medicine · 2024Review
- Control of Peach Leaf Curl with Foliar Applications of Plant Immunity Inducers and Insights in Elicitation of Defense Responses againstJournal of fungi (Basel, Switzerland) · 2024Article
- Letter to the Editor: Cautionary Note on Ribonuclease Activity of Recombinant PR-10 Proteins.Plant & cell physiology · 2023Article
- A novel rubber tree PR-10 protein involved in host-defense response against the white root rot fungus Rigidoporus microporus.BMC plant biology · 2023Article
- Review
- Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1.Foods (Basel, Switzerland) · 2021Article
- Allergens and their associated small molecule ligands-their dual role in sensitization.Allergy · 2021Review
- Structure and Zeatin Binding of the Peach AllergenJournal of agricultural and food chemistry · 2021Article
- Peach allergen Pru p 1 content is generally low in fruit but with large variation in different varieties.Clinical and translational allergy · 2021Article
- Article
- Tiered approach for the identification of Mal d 1 reduced, well tolerated apple genotypes.Scientific reports · 2020Article
- Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family.Current allergy and asthma reports · 2020Review
- Purification and Characterization of Pathogenesis Related Class 10 Panallergens.Foods (Basel, Switzerland) · 2019Article
- Transcriptome Profiles of Strawberry (Frontiers in plant science · 2019Article
- Expression ofPlant direct · 2018Article
- An Ethylene-Induced Regulatory Module Delays Flower Senescence by Regulating Cytokinin Content.Plant physiology · 2017Article
- Identification and Functional Annotation of Genes Differentially Expressed in the Reproductive Tissues of the Olive Tree (Frontiers in plant science · 2017Article
- A first insight into the involvement of phytohormones pathways in coffee resistance and susceptibility to Colletotrichum kahawae.PloS one · 2017Article
- Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response.Acta crystallographica. Section F, Structural biology communications · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PR-10 proteins are a family of pathogenesis-related (PR) allergenic proteins playing multifunctional roles. The peach (Prunus persica) major allergen, Pru p 1.01, and its isoform, Pru p 1.06D, were found highly expressed in the fruit skin at the pit hardening stage, when fruits transiently lose their susceptibility to the fungal pathogen Monilinia spp. To investigate the possible role of the two Pru p 1 isoforms in plant defense, the recombinant proteins were expressed in Escherichia coli and purified. Light scattering experiments and circular dichroism spectroscopy showed that both proteins are monomers in solution with secondary structures typical of PR-10 proteins. Even though the proteins do not display direct antimicrobial activity, they both act as RNases, a function possibly related to defense. The RNase activity is different for the two proteins, and only that of Pru p 1.01 is affected in the presence of the cytokinin zeatin, suggesting a physiological correlation between Pru p 1.01 ligand binding and enzymatic activity. The binding of zeatin to Pru p 1.01 was evaluated using isothermal titration calorimetry, which provided information on the stoichiometry and on the thermodynamic parameters of the interaction. The structural architecture of Pru p 1.01 and Pru p 1.06D was obtained by homology modeling, and the differences in the binding pockets, possibly accounting for the observed difference in binding activity, were evaluated.
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