The Transcription Factor COL12 Is a Substrate of the COP1/SPA E3 Ligase and Regulates Flowering Time and Plant Architecture

Ordoñez-Herrera, Natalia; Trimborn, Laura; Menje, Melanie; Henschel, Monique; Robers, Lennart; Kaufholdt, David; Hänsch, Robert; Adrian, Jessika; Ponnu, Jathish; Hoecker, Ute

doi:10.1104/pp.17.01207

Cited by 56 publications

(43 citation statements)

References 53 publications

(97 reference statements)

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“…Overexpression of AtBBX7 ( COL9 ) induces a delay in flowering under long‐day (LD) conditions through its repression of FT (Cheng and Wang, ; Imtiaz et al , ). AtBBX10 ( COL12 ) delays flowering by repressing CO protein activity (Ordoñez‐Herrera et al , ), while the functions of BBX family members in the groups II (BBX7‐13) are largely unknown in other plants.…”

Section: Introductionmentioning

confidence: 99%

CmBBX8 accelerates flowering by targeting CmFTL1 directly in summer chrysanthemum

Wang

Sun

Ren

et al. 2020

Plant Biotechnology Journal

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Summary For a flowering plant, the transition from vegetative stage to reproductive growth is probably the most critical developmental switch. In the model plant Arabidopsis thaliana, the product of BBX7, group II member of BBX family, acts to delay floral transition. In this study, a presumed chrysanthemum homolog of a second group gene AtBBX8, designated CmBBX8, had been isolated and characterized. The transcription of CmBBX8 followed a diurnal rhythm as the chrysanthemum floral transition regulator. Overexpression of CmBBX8 accelerated flowering, while its (artificial microRNAs) amiR‐enabled knockdown delayed flowering in plants grown under both long‐ and short‐day conditions. Global expression analysis revealed that genes associated with photoperiod were down‐regulated in amiR‐CmBBX8 lines compared with the wild type, which were verified to be up‐regulated in overexpressing lines (OX‐CmBBX8) by RT‐PCR. A number of in vitro assays were used to show that CmBBX8 targets CmFTL1. Furthermore, the function of CmFTL1 as a floral inducer under long‐day conditions was confirmed by the behaviour of engineered summer‐flowering chrysanthemum plants. The conclusion is that the BBX8‐FT regulatory module is an important determinant of reproductive development in summer‐flowering chrysanthemum.

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Section: Introductionmentioning

confidence: 99%

CmBBX8 accelerates flowering by targeting CmFTL1 directly in summer chrysanthemum

Wang

Sun

Ren

et al. 2020

Plant Biotechnology Journal

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“…In addition to HY5, other COP1 targets have been identified including transcriptional regulators, such as the HY5 homolog HYH (Holm et al , ), CONSTANS (CO) and other members of the BBX protein family (Jang et al , ; Liu et al , ; Khanna et al , ; Xu et al , ; Lin et al , ; Ordoñez‐Herrera et al , ), and others such as LONG HYPOCOTYL IN FAR‐RED 1 (HFR1) (Jang et al , ; Yang et al , ) and SHI‐RELATED SEQUENCE 5 (SRS5) (Yuan et al , ). It has been suggested that specific Val‐Pro (VP)‐peptide motifs with a core sequence V‐P‐E/D‐Φ‐G, where Φ designated a hydrophobic residue, are able to bind the COP1 WD40 domain (Holm et al , ; Uljon et al , ).…”

Section: Introductionmentioning

confidence: 99%

Plant photoreceptors and their signaling components compete for COP 1 binding via VP peptide motifs

et al. 2019

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Plants sense different parts of the sun's light spectrum using distinct photoreceptors, which signal through the E3 ubiquitin ligase COP1. Here, we analyze why many COP1‐interacting transcription factors and photoreceptors harbor sequence‐divergent Val‐Pro (VP) motifs that bind COP1 with different 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 COP1. Photoactivation of UVR8 leads to high‐affinity cooperative binding of its VP motif and its photosensing core to COP1, preventing COP1 binding to its substrate HY5. UVR8–VP motif chimeras suggest that UV‐B signaling specificity resides in the UVR8 photoreceptor core. Different COP1–VP peptide motif complexes highlight sequence fingerprints required for COP1 targeting. The blue‐light photoreceptors CRY1 and CRY2 also compete with transcription factors for COP1 binding using similar VP motifs. Thus, our work reveals that different photoreceptors and their signaling components compete for COP1 via a conserved mechanism to control different light signaling cascades.

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“…In addition to HY5, other COP1 targets have been identified including transcriptional regulators, such as the HY5 homolog HYH (Holm et al, 2002), CONSTANS (CO) and other members of the BBX protein family (Jang et al, 2008;Khanna et al, 2009;Xu et al, 2016;Ordoñez-Herrera et al, 2018), and others such as LONG HYPOCOTYL IN FAR-RED (HFR1) (Jang et al, 2005;Yang et al, 2005) and SHI-RELATED SEQUENCE5 (SRS5) (Yuan et al, 2018). It has been suggested that specific Val-Pro (VP)-peptide motifs with a core sequence V-P-E/D-Φ-G, where Φ designated a hydrophobic residue, are able to bind the COP1 WD40 domain (Holm et al, 2001;Uljon et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

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

Lau

Podolec

Chappuis

et al. 2019

Preprint

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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

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The Transcription Factor COL12 Is a Substrate of the COP1/SPA E3 Ligase and Regulates Flowering Time and Plant Architecture

Cited by 56 publications

References 53 publications

CmBBX8 accelerates flowering by targeting CmFTL1 directly in summer chrysanthemum

CmBBX8 accelerates flowering by targeting CmFTL1 directly in summer chrysanthemum

Plant photoreceptors and their signaling components compete for COP 1 binding via VP peptide motifs

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

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