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Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis

Martina K. Ried, Rebekka Wild, Jinsheng Zhu, Larissa Broger, Robert K. Harmel, Ludwig A. Hothorn, Dorothea Fiedler, Michael Hothorn
doi: https://doi.org/10.1101/2019.12.13.875393
Martina K. Ried
1Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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Rebekka Wild
1Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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Jinsheng Zhu
1Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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Larissa Broger
1Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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Robert K. Harmel
2Leibniz-Forschungsinstitut für Molekulare Pharmakologie, 13125 Berlin, Germany & Department of Chemistry, Humboldt-Universität zu Berlin, 12489 Berlin, Germany
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Ludwig A. Hothorn
3Institute of Biostatistics, Leibniz University, 30419 Hannover, Germany
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Dorothea Fiedler
2Leibniz-Forschungsinstitut für Molekulare Pharmakologie, 13125 Berlin, Germany & Department of Chemistry, Humboldt-Universität zu Berlin, 12489 Berlin, Germany
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Michael Hothorn
1Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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  • For correspondence: michael.hothorn@unige.ch
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Abstract

Phosphorus is an essential nutrient taken up by organisms in the form of inorganic phosphate (Pi). Eukaryotes have evolved sophisticated Pi sensing and signalling cascades, enabling them to maintain cellular Pi concentrations. Pi homeostasis is regulated by inositol pyrophosphate signalling molecules (PP-InsPs), which are sensed by SPX-domain containing proteins. In plants, PP-InsP bound SPX receptors inactivate Myb coiled-coil (MYB-CC) Pi starvation response transcription factors (PHRs) by an unknown mechanism. Here we report that a InsP8 – SPX complex targets the plant-unique CC domain of PHRs. Crystal structures of the CC domain reveal an unusual four-stranded anti-parallel arrangement. Interface mutations in the CC domain yield monomeric PHR1, which is no longer able to bind DNA with high affinity. Mutation of conserved basic residues located at the surface of the CC domain disrupt interaction with the SPX receptor in vitro and in planta, resulting in constitutive Pi starvation responses. Together, our findings suggest that InsP8 regulates plant Pi homeostasis by controlling the oligomeric state and hence the promoter binding capability of PHRs via their SPX receptors. (173 words)

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Posted December 13, 2019.
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Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis
Martina K. Ried, Rebekka Wild, Jinsheng Zhu, Larissa Broger, Robert K. Harmel, Ludwig A. Hothorn, Dorothea Fiedler, Michael Hothorn
bioRxiv 2019.12.13.875393; doi: https://doi.org/10.1101/2019.12.13.875393
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Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis
Martina K. Ried, Rebekka Wild, Jinsheng Zhu, Larissa Broger, Robert K. Harmel, Ludwig A. Hothorn, Dorothea Fiedler, Michael Hothorn
bioRxiv 2019.12.13.875393; doi: https://doi.org/10.1101/2019.12.13.875393

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