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

Research output: Contribution to journalJournal articleResearchpeer-review

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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 journalJournal articleResearchpeer-review

Harvard

Altensell, J, Wartenberg, R, Haferkamp, I, Hassler, S, Scherer, V, Steensma, P, Fitzpatrick, TB, Sharma, A, Sandoval-Ibanez, O, Pribil, M, Lehmann, M, Leister, D, Kleine, T & Neuhaus, HE 2022, 'Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier', Plant Physiology, vol. 189, no. 1, pp. 49-65. https://doi.org/10.1093/plphys/kiac048

APA

Altensell, J., Wartenberg, R., Haferkamp, I., Hassler, S., Scherer, V., Steensma, P., Fitzpatrick, T. B., Sharma, A., Sandoval-Ibanez, O., Pribil, M., Lehmann, M., Leister, D., Kleine, T., & Neuhaus, H. E. (2022). Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier. Plant Physiology, 189(1), 49-65. https://doi.org/10.1093/plphys/kiac048

Vancouver

Altensell J, Wartenberg R, Haferkamp I, Hassler S, Scherer V, Steensma P et al. Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier. Plant Physiology. 2022;189(1):49-65. https://doi.org/10.1093/plphys/kiac048

Author

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. / Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier. In: Plant Physiology. 2022 ; Vol. 189, No. 1. pp. 49-65.

Bibtex

@article{f17a3575d625417d98d30f12c0c62264,
title = "Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier",
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.",
keywords = "ADENINE-NUCLEOTIDE TRANSPORTER, ATP/ADP TRANSPORTERS, PHOTORESPIRATION, SUPERFAMILY, VITAMIN-B-6, METABOLISM, PROTEIN, TRANSLOCATION, BIOSYNTHESIS, DIVERSITY",
author = "Jacqueline Altensell and Ruth Wartenberg and Ilka Haferkamp and Sebastian Hassler and Vanessa Scherer and Priscille Steensma and Fitzpatrick, {Teresa B.} and Anurag Sharma and Omar Sandoval-Ibanez and Mathias Pribil and Martin Lehmann and Dario Leister and Tatjana Kleine and Neuhaus, {H. Ekkehard}",
year = "2022",
doi = "10.1093/plphys/kiac048",
language = "English",
volume = "189",
pages = "49--65",
journal = "Plant Physiology",
issn = "0032-0889",
publisher = "American Society of Plant Biologists",
number = "1",

}

RIS

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