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Int. J. Mol. Sci. 2019, 20(8), 1889; https://doi.org/10.3390/ijms20081889

The Major Storage Protein in Potato Tuber Is Mobilized by a Mechanism Dependent on Its Phosphorylation Status

1
Department of Zoology, Genetics and Physical Anthropology, University of Santiago de Compostela, 15782 Santiago de Compostela, Spain
2
Meat Technology Center of Galicia, 32900 San Cibrao das Viñas, Ourense, Spain
*
Author to whom correspondence should be addressed.
Received: 21 February 2019 / Revised: 5 April 2019 / Accepted: 13 April 2019 / Published: 17 April 2019
(This article belongs to the Special Issue Plant Proteomic Research 2.0)
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Abstract

The role of the protein phosphorylation mechanism in the mobilization of vegetative storage proteins (VSPs) is totally unknown. Patatin is the major VSP of the potato (Solanum tuberosum L.) tuber that encompasses multiple differentially phosphorylated isoforms. In this study, temporal changes in the phosphorylation status of patatin isoforms and their involvement in patatin mobilization are investigated using phosphoproteomic methods based on targeted two-dimensional electrophoresis (2-DE). High-resolution 2-DE profiles of patatin isoforms were obtained in four sequential tuber life cycle stages of Kennebec cultivar: endodormancy, bud break, sprouting and plant growth. In-gel multiplex identification of phosphorylated isoforms with Pro-Q Diamond phosphoprotein-specific stain revealed an increase in the number of phosphorylated isoforms after the tuber endodormancy stage. In addition, we found that the phosphorylation status of patatin isoforms significantly changed throughout the tuber life cycle (P < 0.05) using the chemical method of protein dephosphorylation with hydrogen fluoride-pyridine (HF-P) coupled to 2-DE. More specifically, patatin phosphorylation increased by 32% from endodormancy to the tuber sprouting stage and subsequently decreased together with patatin degradation. Patatin isoforms were not randomly mobilized because highly phosphorylated Kuras-isoforms were preferably degraded in comparison to less phosphorylated non-Kuras isoforms. These results lead us to conclude that patatin is mobilized by a mechanism dependent on the phosphorylation status of specific isoforms. View Full-Text
Keywords: Solanum tuberosum; patatin; seed storage proteins; vegetative storage proteins; tuber phosphoproteome; targeted two-dimensional electrophoresis Solanum tuberosum; patatin; seed storage proteins; vegetative storage proteins; tuber phosphoproteome; targeted two-dimensional electrophoresis
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Bernal, J.; Mouzo, D.; López-Pedrouso, M.; Franco, D.; García, L.; Zapata, C. The Major Storage Protein in Potato Tuber Is Mobilized by a Mechanism Dependent on Its Phosphorylation Status. Int. J. Mol. Sci. 2019, 20, 1889.

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