Pi starvation-dependent regulation of ethanolamine metabolism by phosphoethanolamine phosphatase PECP1 in Arabidopsis roots

© The Author(s) 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 69(2018), 3 vom: 23. Jan., Seite 467-481
1. Verfasser: Tannert, Martin (VerfasserIn)
Weitere Verfasser: May, Anett, Ditfe, Daniela, Berger, Sigrid, Balcke, Gerd Ulrich, Tissier, Alain, Köck, Margret
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Choline PECP1 ethanolamine hydrophilic interaction chromatography (HILIC) phosphatase phosphate starvation phosphocholine phosphoethanolamine mehr... phospholipid Ethanolamines Phosphates Phosphorylcholine 107-73-3 Ethanolamine 5KV86114PT phosphorylethanolamine 78A2BX7AEU PECP1 protein, Arabidopsis EC 3.1.3.- Phosphoric Monoester Hydrolases EC 3.1.3.2
Beschreibung
Zusammenfassung:© The Author(s) 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.
A universal plant response to phosphorus deprivation is the up-regulation of a diverse array of phosphatases. As reported recently, the AtPECP1 gene encodes a phosphatase with in vitro substrate specificity for phosphoethanolamine and phosphocholine. The putative substrates suggested that AtPECP1 is related to phospholipid metabolism; however, the biological function of AtPECP1 is as yet not understood. In addition, whereas lipid remodelling processes as part of the phosphorus starvation response have been extensively studied, knowledge of the polar head group metabolism and its regulation is lacking. We found that AtPECP1 is expressed in the cytosol and exerts by far its strongest activity in roots of phosphate-starved plants. We established a novel LC-MS/MS-based method for the quantitative and simultaneous measurement of the head group metabolites. The analysis of Atpecp1 null mutants and overexpression lines revealed that phosphoethanolamine, but not phosphocholine is the substrate of AtPECP1 in vivo. The impact on head group metabolite levels is greatest in roots of both loss-of-function and gain-of-function transgenic lines, indicating that the biological role of AtPECP1 is mainly restricted to roots. We suggest that phosphoethanolamine hydrolysis by AtPECP1 during Pi starvation is required to down-regulate the energy-consuming biosynthesis of phosphocholine through the methylation pathway
Beschreibung:Date Completed 14.05.2019
Date Revised 14.05.2019
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erx408