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Plant photoreceptors and their signaling components compete for binding to the ubiquitin ligase COP1 using their VP-peptide motifs

View ORCID ProfileKelvin Lau, View ORCID ProfileRoman Podolec, Richard Chappuis, View ORCID ProfileRoman Ulm, View ORCID ProfileMichael Hothorn
doi: https://doi.org/10.1101/568618
Kelvin Lau
1Department of Botany and Plant Biology, Section of Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland
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Roman Podolec
1Department of Botany and Plant Biology, Section of Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland
2Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva, Geneva, Switzerland
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Richard Chappuis
1Department of Botany and Plant Biology, Section of Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland
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Roman Ulm
1Department of Botany and Plant Biology, Section of Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland
2Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva, Geneva, Switzerland
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  • For correspondence: roman.ulm@unige.ch michael.hothorn@unige.ch
Michael Hothorn
1Department of Botany and Plant Biology, Section of Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland
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  • For correspondence: roman.ulm@unige.ch michael.hothorn@unige.ch
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SUMMARY

Plants sense different parts of the sun’s light spectrum using specialized photoreceptors, many of which signal through the E3 ubiquitin ligase COP1. Photoreceptor binding modulates COP1’s ubiquitin ligase activity towards transcription factors. Here we analyze why many COP1-interacting transcription factors and photoreceptors harbor sequence-divergent Val-Pro (VP) peptide motifs. We demonstrate that VP motifs enable different light signaling components to bind to the WD40 domain of COP1 with various binding affinities. Crystal structures of the VP motifs of the UV-B photoreceptor UVR8 and the transcription factor HY5 in complex with COP1, quantitative binding assays and reverse genetic experiments together suggest that UVR8 and HY5 compete for the COP1 WD40 domain. Photoactivation of UVR8 leads to high-affinity cooperative binding of its VP domain and its photosensing core to COP1, interfering with the binding of COP1 to its substrate HY5. Functional UVR8 – VP motif chimeras suggest that UV-B signaling specificity resides in the UVR8 photoreceptor core, not its VP motif. Crystal structures of different COP1 – VP peptide complexes highlight sequence fingerprints required for COP1 targeting. The functionally distinct blue light receptors CRY1 and CRY2 also compete with downstream transcription factors for COP1 binding using similar VP-peptide motifs. Together, our work reveals that photoreceptors and their components compete for COP1 using a conserved displacement mechanism to control different light signaling cascades in plants.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted March 05, 2019.
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Plant photoreceptors and their signaling components compete for binding to the ubiquitin ligase COP1 using their VP-peptide motifs
Kelvin Lau, Roman Podolec, Richard Chappuis, Roman Ulm, Michael Hothorn
bioRxiv 568618; doi: https://doi.org/10.1101/568618
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Plant photoreceptors and their signaling components compete for binding to the ubiquitin ligase COP1 using their VP-peptide motifs
Kelvin Lau, Roman Podolec, Richard Chappuis, Roman Ulm, Michael Hothorn
bioRxiv 568618; doi: https://doi.org/10.1101/568618

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