Initiation of cytosolic plant purine nucleotide catabolism involves a monospecific xanthosine monophosphate phosphatase

Katharina J. Heinemann, Sun-Young Yang, Henryk Straube, Nieves Medina-Escobar, Marina Varbanova-Herde, Marco Herde, Sangkee Rhee () and Claus-Peter Witte ()
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Katharina J. Heinemann: Leibniz Universität Hannover, Department of Molecular Nutrition and Biochemistry of Plants
Sun-Young Yang: Seoul National University, Department of Agricultural Biotechnology
Henryk Straube: Leibniz Universität Hannover, Department of Molecular Nutrition and Biochemistry of Plants
Nieves Medina-Escobar: Leibniz Universität Hannover, Department of Molecular Nutrition and Biochemistry of Plants
Marina Varbanova-Herde: Leibniz Universität Hannover, Department of Molecular Nutrition and Biochemistry of Plants
Marco Herde: Leibniz Universität Hannover, Department of Molecular Nutrition and Biochemistry of Plants
Sangkee Rhee: Seoul National University, Department of Agricultural Biotechnology
Claus-Peter Witte: Leibniz Universität Hannover, Department of Molecular Nutrition and Biochemistry of Plants

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: Abstract In plants, guanosine monophosphate (GMP) is synthesized from adenosine monophosphate via inosine monophosphate and xanthosine monophosphate (XMP) in the cytosol. It has been shown recently that the catabolic route for adenylate-derived nucleotides bifurcates at XMP from this biosynthetic route. Dephosphorylation of XMP and GMP by as yet unknown phosphatases can initiate cytosolic purine nucleotide catabolism. Here we show that Arabidopsis thaliana possesses a highly XMP-specific phosphatase (XMPP) which is conserved in vascular plants. We demonstrate that XMPP catalyzes the irreversible entry reaction of adenylate-derived nucleotides into purine nucleotide catabolism in vivo, whereas the guanylates enter catabolism via an unidentified GMP phosphatase and guanosine deaminase which are important to maintain purine nucleotide homeostasis. We also present a crystal structure and mutational analysis of XMPP providing a rationale for its exceptionally high substrate specificity, which is likely required for the efficient catalysis of the very small XMP pool in vivo.

Date: 2021
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DOI: 10.1038/s41467-021-27152-4

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