한빛사 논문
Eunju Kwon,1,4 Deepak Pathak,1,4 Pawan Dahal,1,4 Sudarshan Tandukar,1 Hyun Suk Jung,2 Woe-Yeon Kim,3 and Dong Young Kim1,5,*
1College of Pharmacy, Yeungnam University, Gyeongsan 38541, Republic of Korea
2Department of Biochemistry, College of Natural Sciences, Kangwon National University, Chunchon 24341, Republic of Korea
3Division of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, Republic of Korea
4These authors contributed equally
5Lead contact
*Correspondence
Abstract
In Arabidopsis, GIGANTEA (GI), together with the blue-light receptors ZTL, LKP2, and FKF1, regulates degradation of the core clock protein TOC1 and the flowering repressor CDFs, thereby controlling circadian oscillation and flowering. Despite the significance of GI in diverse plant physiology, its molecular function is not much understood because of technical problems in protein preparation and a lack of structural information. Here, we report the purification of the GI monomer and the crystal structure of the GI/LKP2 complex. The crystal structure reveals that residues 1–813 of GI possess an elongated rigid structure formed by stacking hydrophobic α-helices and that the LOV domain of LKP2 binds to the middle region of the GI (residues 563–789). Interaction analysis further shows that LOV homodimers are converted to monomers by GI binding. Our results provide structural insights into the regulation of the circadian clock and photoperiodic flowering by GI and ZTL/LKP2/FKF1.
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