Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier
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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; Neuhaus, H. Ekkehard.
In: Plant Physiology, Vol. 189, No. 1, 2022, p. 49-65.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier
AU - Altensell, Jacqueline
AU - Wartenberg, Ruth
AU - Haferkamp, Ilka
AU - Hassler, Sebastian
AU - Scherer, Vanessa
AU - Steensma, Priscille
AU - Fitzpatrick, Teresa B.
AU - Sharma, Anurag
AU - Sandoval-Ibanez, Omar
AU - Pribil, Mathias
AU - Lehmann, Martin
AU - Leister, Dario
AU - Kleine, Tatjana
AU - Neuhaus, H. Ekkehard
PY - 2022
Y1 - 2022
N2 - 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.
AB - 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.
KW - ADENINE-NUCLEOTIDE TRANSPORTER
KW - ATP/ADP TRANSPORTERS
KW - PHOTORESPIRATION
KW - SUPERFAMILY
KW - VITAMIN-B-6
KW - METABOLISM
KW - PROTEIN
KW - TRANSLOCATION
KW - BIOSYNTHESIS
KW - DIVERSITY
U2 - 10.1093/plphys/kiac048
DO - 10.1093/plphys/kiac048
M3 - Journal article
C2 - 35139220
VL - 189
SP - 49
EP - 65
JO - Plant Physiology
JF - Plant Physiology
SN - 0032-0889
IS - 1
ER -
ID: 300774244