Identification of the ligand of Pru p 3, a peach LTP

Nuria Cubells-Baeza, Cristina Gómez-Casado, Leticia Tordesillas, Carmen Ramírez-Castillejo, María Garrido-Arandia, Pablo González-Melendi, María Herrero, Luis F. Pacios, Araceli Díaz-Perales

Research output: Contribution to journalArticlepeer-review

Abstract

Key message: Pru p 3, a peach LTP, is located in pollinated flower styles and secreting downy hairs, transporting a derivative of camptothecin bound to phytosphingosine. Pru p 3 may inhibit a second pollination and may keep away herbivores until seed maturation. Abstract: The allergen Pru p 3, a peach lipid transfer protein, has been well studied. However, its physiological function remains to be elucidated. Our results showed that Pru p 3 usually carries a lipid ligand that play an essential role in its function in plants. Using ESI-qToF, we observed that the ligand was a derivative of camptothecin binding to phytosphingosine, wich that is inserted into the hydrophobic tunnel of the protein. In addition, the described ligand displayed topoisomerase I activity inhibition and self-fluorescence, both recognized as camptothecin properties. During flower development, the highest expression of Pru p 3 was detected in the styles of pollinated flowers, in contrast to its non-expression in unpollinated pistils, where expression decreased after anthesis. During ripening, the expression of Pru p 3 were observed mainly in peel but not in pulp. In this sense, Pru p 3 protein was also localized in trichomes covering the fruit epidermis.

Original languageEnglish
Pages (from-to)33-44
Number of pages12
JournalPlant Molecular Biology
Volume94
Issue number1-2
Early online date2017 Mar 15
DOIs
Publication statusPublished - 2017 May

Subject classification (UKÄ)

  • Biochemistry and Molecular Biology
  • Botany

Free keywords

  • Camptothecin
  • Flower development
  • Fruit development
  • Lipid transfer protein
  • Pollination
  • Pru p 3
  • Secondary metabolites

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