Sweet Cherry (Prunus avium L.) PaPIP1;4 is a functional aquaporin upregulated by pre-harvest calcium treatments that prevent cracking

• Published in: International journal of molecular sciences Vol. 21; no. 8; p. 3017
• Main Authors: Breia, Richard Maykel Gonçalves, Mósca, Andreia F., Conde, Artur, Correia, Sofia, Conde, Carlos, Noronha, Henrique, Soveral, Graça, Gonçalves, Berta, Gerós, H.
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI 24-04-2020; MDPI AG
• Subjects: Amino Acid Sequence; Amino acids; Aquaporins; Aquaporins - genetics; Aquaporins - metabolism; Calcium - metabolism; calcium application; Calcium chloride; Cell adhesion & migration; Cloning, Molecular; Computational Biology - methods; Cultivars; Fruit - metabolism; fruit-cracking; Fruits; Genomes; Hydrogen peroxide; Hypotheses; Localization; Membrane proteins; Membranes; Mutation; PaPIP1; Permeability; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Proteins - metabolism; Plasma; Protein transport; Proteins; Prunus avium; Prunus avium - physiology; Rain; Science & Technology; Sequence Analysis, DNA; Studies; sweet-cherry; Tobacco; Transcription; Transport; aquaporins; sweet-cherry; PaPIP1; fruit-cracking; 4; calcium application
• ISSN: 1422-0067; 1661-6596; 1661-6596; 1422-0067
• DOI: 10.3390/ijms21083017

The involvement of aquaporins in rain-induced sweet cherry (Prunus avium L.) fruit cracking is an important research topic with potential agricultural applications. In the present study, we performed the functional characterization of PaPIP1;4, the most expressed aquaporin in sweet cherry fruit. Field experiments focused on the pre-harvest exogenous application to sweet cherry trees, cultivar Skeena, with a solution of 0.5% CaCl2, which is the most common treatment to prevent cracking. Results show that PaPIP1;4 was mostly expressed in the fruit peduncle, but its steady-state transcript levels were higher in fruits from CaCl2-treated plants than in controls. The transient expression of PaPIP1;4-GFP in tobacco epidermal cells and the overexpression of PaPIP1;4 in YSH1172 yeast mutation showed that PaPIP1;4 is a plasma membrane protein able to transport water and hydrogen peroxide. In this study, we characterized for the first time a plasma membrane sweet cherry aquaporin able to transport water and H2O2 that is upregulated by the pre-harvest exogenous application of CaCl2 supplements.
This work was supported by the “Contrato-Programa” UIDB/04050/2020 and UIDB/04033/2020 funded by national funds through the FCT I.P. The work was also supported by FCT and European Funds (FEDER/POCI/COMPETE2020) through the research projects MitiVineDrought (PTDC/BIA-FBT/30341/2017 and POCI-01-0145-FEDER-030341), BerryPlastid (PTDC/BIA-FBT/28165/2017 and POCI-01-0145-FEDER-028165) and CherryCrackLess (PTDC/AGR-PRO/7028/2014). R.B. was supported with a PhD student grant (PD/BD/113616/2015) under the Agrichains Doctoral Program (PD/00122/2012) funded by FCT. H.N. was supported by an FCT postdoctoral grant (SFRH/BPD/115518/2016) and A.C. was supported by a contract in the MitiVineDrought project.