The F-box protein FKF1 inhibits dimerization of COP1 in the control of photoperiodic floweringopen access
- Authors
- Lee, Byoung-Doo; Kim, Mi Ri; Kang, Min-Young; Cha, Joon-Yung; Han, Su-Hyun; Nawkar, Ganesh M.; Sakuraba, Yasuhito; Lee, Sang Yeol; Imaizumi, Takato; McClung, C. Robertson; Kim, Woe-Yeon; Paek, Nam-Chon
- Issue Date
- 22-Dec-2017
- Publisher
- NATURE PORTFOLIO
- Citation
- NATURE COMMUNICATIONS, v.8
- Indexed
- SCI
SCIE
SCOPUS
- Journal Title
- NATURE COMMUNICATIONS
- Volume
- 8
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/13269
- DOI
- 10.1038/s41467-017-02476-2
- ISSN
- 2041-1723
2041-1723
- Abstract
- 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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