Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier

Altensell, Jacqueline; Wartenberg, Ruth; Haferkamp, Ilka; Hassler, Sebastian; Scherer, Vanessa; Steensma, Priscille; Fitzpatrick, Teresa B.; Sharma, Anurag; Sandoval-Ibanez, Omar; Pribil, Mathias; Lehmann, Martin; Leister, Dario; Kleine, Tatjana und Neuhaus, H. Ekkehard (2022): Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier. In: Plant Physiology, Bd. 189, Nr. 1: S. 49-65

Abstract

Knocking out the activity of a pyridoxal 5 '-phosphate phosphatase suppresses the dwarf phenotype of mutants lacking an ATP/ADP transporter and provides insight into vitamin B6 homeostasis. The endoplasmic reticulum (ER)-located ATP/ADP-antiporter (ER-ANT1) occurs specifically in vascular plants. Structurally different transporters mediate energy provision to the ER, but the cellular function of ER-ANT1 is still unknown. Arabidopsis (Arabidopsis thaliana) mutants lacking ER-ANT1 (er-ant1 plants) exhibit a photorespiratory phenotype accompanied by high glycine levels and stunted growth, pointing to an inhibition of glycine decarboxylase (GDC). To reveal whether it is possible to suppress this marked phenotype, we exploited the power of a forward genetic screen. Absence of a so far uncharacterized member of the HaloAcid Dehalogenase (HAD)-like hydrolase family strongly suppressed the dwarf phenotype of er-ant1 plants. Localization studies suggested that the corresponding protein locates to chloroplasts, and activity assays showed that the enzyme dephosphorylates, with high substrate affinity, the B-6 vitamer pyridoxal 5 '-phosphate (PLP). Additional physiological experiments identified imbalances in vitamin B-6 homeostasis in er-ant1 mutants. Our data suggest that impaired chloroplast metabolism, but not decreased GDC activity, causes the er-ant1 mutant dwarf phenotype. We present a hypothesis, setting transport of PLP by ER-ANT1 and chloroplastic PLP dephosphorylation in the cellular context. With the identification of this HAD-type PLP phosphatase, we also provide insight into B-6 vitamer homeostasis.

• Dokumententyp: Zeitschriftenartikel
• Fakultät: Biologie
• Themengebiete: 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
• ISSN: 0032-0889
• Sprache: Englisch