GIGANTEA is a co-chaperone which facilitates maturation of ZEITLUPE in the Arabidopsis circadian clock

被引:149
作者
Cha, Joon-Yung [1 ]
Kim, Jeongsik [2 ,3 ]
Kim, Tae-Sung [2 ,4 ]
Zeng, Qingning [2 ]
Wang, Lei [2 ,5 ]
Lee, Sang Yeol [1 ]
Kim, Woe-Yeon [1 ]
Somers, David E. [2 ]
机构
[1] Gyeongsang Natl Univ, PMBBRC & IALS, Div Appl Life Sci, BK21Plus, Jinju 52828, South Korea
[2] Ohio State Univ, Dept Mol Genet, Columbus, OH 43210 USA
[3] Inst Basic Sci, Ctr Plant Aging Res, Daegu 711873, South Korea
[4] Korea Natl Open Univ, Dept Agr Sci, Seoul 03087, South Korea
[5] Chinese Acad Sci, Inst Bot, Key Lab Plant Mol Physiol, Beijing 100093, Peoples R China
来源
NATURE COMMUNICATIONS | 2017年 / 8卷
基金
美国国家卫生研究院;
关键词
BOX PROTEIN ZEITLUPE; IN-VITRO; POSTTRANSLATIONAL REGULATION; FUNCTIONAL-CHARACTERIZATION; TARGETED DEGRADATION; REGULATOR PROTEINS; SCFZTL COMPLEX; BLUE-LIGHT; HSP90; THALIANA;
D O I
10.1038/s41467-016-0014-9
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Circadian clock systems help establish the correct daily phasing of the behavioral, developmental, and molecular events needed for the proper coordination of physiology and metabolism. The circadian oscillator comprises transcription-translation feedback loops but also requires post-translational processes that regulate clock protein homeostasis. GIGANTEA is a unique plant protein involved in the maintenance and control of numerous facets of plant physiology and development. Through an unknown mechanism GIGANTEA stabilizes the F-box protein ZEITLUPE, a key regulator of the circadian clock. Here, we show that GIGANTEA has general protein chaperone activity and can act to specifically facilitate ZEITLUPE maturation into an active form in vitro and in planta. GIGANTEA forms a ternary complex with HSP90 and ZEITLUPE and its co-chaperone action synergistically enhances HSP90/HSP70 maturation of ZEITLUPE in vitro. These results identify a molecular mechanism for GIGANTEA activity that can explain its wide-ranging role in plant biology.
引用
收藏
页数:12
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