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Arabidopsis PFA-DSP-Type Phosphohydrolases Target Specific Inositol Pyrophosphate Messengers

Gaugler, P and Schneider, R and Liu, G and Qiu, D and Weber, J and Schmid, J and Jork, N and Häner, M and Ritter, K and Fernández-Rebollo, N and Giehl, RFH and Trung, MN and Yadav, R and Fiedler, D and Gaugler, V and Jessen, HJ and Schaaf, G and Laha, D (2022) Arabidopsis PFA-DSP-Type Phosphohydrolases Target Specific Inositol Pyrophosphate Messengers. In: Biochemistry, 61 (12). pp. 1213-1227.

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Official URL: https://doi.org/10.1021/acs.biochem.2c00145


Inositol pyrophosphates are signaling molecules containing at least one phosphoanhydride bond that regulate a wide range of cellular processes in eukaryotes. With a cyclic array of phosphate esters and diphosphate groups around myo-inositol, these molecular messengers possess the highest charge density found in nature. Recent work deciphering inositol pyrophosphate biosynthesis in Arabidopsis revealed important functions of these messengers in nutrient sensing, hormone signaling, and plant immunity. However, despite the rapid hydrolysis of these molecules in plant extracts, very little is known about the molecular identity of the phosphohydrolases that convert these messengers back to their inositol polyphosphate precursors. Here, we investigate whether Arabidopsis Plant and Fungi Atypical Dual Specificity Phosphatases (PFA-DSP1-5) catalyze inositol pyrophosphate phosphohydrolase activity. We find that recombinant proteins of all five Arabidopsis PFA-DSP homologues display phosphohydrolase activity with a high specificity for the 5-β-phosphate of inositol pyrophosphates and only minor activity against the β-phosphates of 4-InsP7and 6-InsP7. We further show that heterologous expression of Arabidopsis PFA-DSP1-5 rescues wortmannin sensitivity and deranged inositol pyrophosphate homeostasis caused by the deficiency of the PFA-DSP-type inositol pyrophosphate phosphohydrolase Siw14 in yeast. Heterologous expression in Nicotiana benthamiana leaves provided evidence that Arabidopsis PFA-DSP1 also displays 5-β-phosphate-specific inositol pyrophosphate phosphohydrolase activity in planta. Our findings lay the biochemical basis and provide the genetic tools to uncover the roles of inositol pyrophosphates in plant physiology and plant development.

Item Type: Journal Article
Publication: Biochemistry
Publisher: American Chemical Society
Additional Information: The copyright for this article belongs to the Author(s).
Keywords: Alcohols; Biochemistry; Digital signal processing; Molecules; Physiology; Plant extracts; Polyols; Recombinant proteins, Arabidopsis; Cellular process; Heterologous expression; High charges; Inositol pyrophosphate; Myo-inositol; Phosphate esters; Phosphoanhydride; Phosphohydrolases; Signaling molecules, Sugars, diphosphoric acid; dual specificity phosphatase; inositol phosphate; pyrophosphate, Arabidopsis; genetics; metabolism; Saccharomyces cerevisiae, Arabidopsis; Diphosphates; Dual-Specificity Phosphatases; Inositol Phosphates; Saccharomyces cerevisiae
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 21 Sep 2022 08:57
Last Modified: 21 Sep 2022 08:57
URI: https://eprints.iisc.ac.in/id/eprint/76616

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