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Plant photoreceptors and their signaling components compete for COP1 binding via VP peptide motifs.
The EMBO Journal ( IF 9.4 ) Pub Date : 2019-07-15 , DOI: 10.15252/embj.2019102140
Kelvin Lau 1 , Roman Podolec 1, 2 , Richard Chappuis 1 , Roman Ulm 1, 2 , Michael Hothorn 1
Affiliation  

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.

中文翻译:

植物光感受器及其信号成分通过VP肽基元竞争COP1结合。

植物使用不同的感光器来感知太阳光谱的不同部分,这些感光器通过E3泛素连接酶COP1发出信号。在这里,我们分析了为什么许多与COP1相互作用的转录因子和光感受器都带有以不同亲和力结合COP1的序列不同的Val-Pro(VP)图案。与COP1配合使用的UV-B感光体UVR8和转录因子HY5的VP基序的晶体结构,定量结合测定和反向遗传实验共同表明,UVR8和HY5竞争COP1。UVR8的光活化导致其VP基序及其光敏核心与COP1高亲和力协同结合,从而阻止COP1与其底物HY5结合。UVR8-VP基序嵌合体表明UV-B信号传导特异性位于UVR8感光核中。不同的COP1-VP肽基序复合物突出显示COP1靶向所需的序列指纹。蓝光感光体CRY1和CRY2也与转录因子竞争使用相似VP基序的COP1结合。因此,我们的工作揭示了不同的光感受器及其信号成分通过保守机制竞争COP1,以控制不同的光信号级联反应。
更新日期:2019-09-16
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