Ponnu, Jathish ORCID: 0000-0002-3276-7068, Riedel, Tabea, Penner, Eva, Schrader, Andrea ORCID: 0000-0002-3879-7057 and Hoecker, Ute ORCID: 0000-0002-5636-9777 (2019). Cryptochrome 2 competes with COP1 substrates to repress COP1 ubiquitin ligase activity during Arabidopsis photomorphogenesis. Proc. Natl. Acad. Sci. U. S. A., 116 (52). S. 27133 - 27142. WASHINGTON: NATL ACAD SCIENCES. ISSN 0027-8424

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Abstract

In plants, the cryptochrome photoreceptors suppress the activity of the COP1 /SPA ubiquitin ligase to initiate photomorphogenesis in blue light. Both CRY1 and CRY2 interact with the COP1/SPA complex in a blue light-dependent manner. The mechanisms underlying the inhibition of COP1 activity through direct interactions with photoactivated CRYs are not fully understood. Here we tested the hypothesis that CRY2 inhibits COP1 by displacing the degradation substrates from COP1. To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1. We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast twohybrid assays and in planta. Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP. The interaction between COP1 and its VP-containing substrate PAP2 was prevented in the presence of coexpressed CRY2, but not in the presence of CRY2 carrying a VP mutation. Thus, since both PAP2 and CRY2 engage VP motifs to bind to COP1, these results demonstrate that CRY2 outcompetes PAP2 for binding to COP1. We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains. A VP motif present in CRY1 is also essential for binding to COP1. Thus, CRY1 and CRY2 might share this mechanism of COP1 inactivation.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Ponnu, JathishUNSPECIFIEDorcid.org/0000-0002-3276-7068UNSPECIFIED
Riedel, TabeaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Penner, EvaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Schrader, AndreaUNSPECIFIEDorcid.org/0000-0002-3879-7057UNSPECIFIED
Hoecker, UteUNSPECIFIEDorcid.org/0000-0002-5636-9777UNSPECIFIED
URN: urn:nbn:de:hbz:38-123945
DOI: 10.1073/pnas.1909181116
Journal or Publication Title: Proc. Natl. Acad. Sci. U. S. A.
Volume: 116
Number: 52
Page Range: S. 27133 - 27142
Date: 2019
Publisher: NATL ACAD SCIENCES
Place of Publication: WASHINGTON
ISSN: 0027-8424
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Biology > Botanical Institute
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
LIGHT-DEPENDENT INTERACTION; ANTHOCYANIN ACCUMULATION; SIGNALING MECHANISMS; FLORAL INITIATION; REPEAT DOMAIN; SPA1; TRANSCRIPTION; PROTEINS; PHYTOCHROME; INTERACTMultiple languages
Multidisciplinary SciencesMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/12394

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