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The F-box protein FKF1 inhibits dimerization of COP1 in the control of photoperiodic flowering.

Byoung-Doo LeeMi Ri KimMin-Young KangJoon-Yung ChaSu-Hyun HanGanesh M NawkarYasuhito SakurabaSang Yeol LeeTakato ImaizumiC Robertson McClungWoe-Yeon KimNam-Chon Paek
Published in: Nature communications (2017)
In Arabidopsis thaliana, CONSTANS (CO) plays an essential role in the regulation of photoperiodic flowering under long-day conditions. CO protein is stable only in the afternoon of long days, when it induces the expression of FLOWERING LOCUS T (FT), which promotes flowering. The blue-light photoreceptor FLAVIN-BINDING, KELCH REPEAT, F-BOX1 (FKF1) interacts with CO and stabilizes it by an unknown mechanism. Here, we provide genetic and biochemical evidence that FKF1 inhibits CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1)-dependent CO degradation. Light-activated FKF1 has no apparent effect on COP1 stability but can interact with and negatively regulate COP1. We show that FKF1 can inhibit COP1 homo-dimerization. Mutation of the coiled-coil domain in COP1, which prevents dimer formation, impairs COP1 function in coordinating flowering time. Based on these results, we propose a model whereby the light- and day length-dependent interaction between FKF1 and COP1 controls CO stability to regulate flowering time.
Keyphrases
  • arabidopsis thaliana
  • binding protein
  • transcription factor
  • poor prognosis
  • genome wide
  • magnetic resonance imaging
  • dna methylation
  • magnetic resonance
  • long non coding rna
  • dna binding