4.8 Article

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

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NATURE COMMUNICATIONS
卷 8, 期 -, 页码 -

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NATURE PORTFOLIO
DOI: 10.1038/s41467-017-02476-2

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资金

  1. Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Science, ICT and Future Planning [NRF-2017R1A2B3003310, NRF-2015R1D1A1A01060604]
  2. Cooperative Research Program for Agriculture Science & Technology Development [PJ010953042017]
  3. Next-Generation BioGreen21 Program (SSAC), Rural Development Administration, Republic of Korea [PJ01106904]
  4. National Institutes of Health Grant, USA [R01 GM079712]
  5. Rural Development Administration (RDA), Republic of Korea [PJ010953042017] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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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.

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