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A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis

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  • Jae-Hoon Jung

    (University of Cambridge
    Sungkyunkwan University)

  • Antonio D. Barbosa

    (University of Cambridge)

  • Stephanie Hutin

    (Université Grenoble Alpes/CNRS/CEA/INRAE)

  • Janet R. Kumita

    (University of Cambridge
    University of Cambridge)

  • Mingjun Gao

    (University of Cambridge)

  • Dorothee Derwort

    (University of Cambridge)

  • Catarina S. Silva

    (Université Grenoble Alpes/CNRS/CEA/INRAE)

  • Xuelei Lai

    (University of Cambridge
    Université Grenoble Alpes/CNRS/CEA/INRAE)

  • Elodie Pierre

    (Université Grenoble Alpes/CNRS/CEA/INRAE)

  • Feng Geng

    (University of Cambridge)

  • Sol-Bi Kim

    (Sungkyunkwan University)

  • Sujeong Baek

    (Sungkyunkwan University)

  • Chloe Zubieta

    (Université Grenoble Alpes/CNRS/CEA/INRAE)

  • Katja E. Jaeger

    (University of Cambridge
    Leibniz-Institut für Gemüse- und Zierpflanzenbau)

  • Philip A. Wigge

    (University of Cambridge
    Leibniz-Institut für Gemüse- und Zierpflanzenbau
    University of Potsdam)

Abstract

Temperature controls plant growth and development, and climate change has already altered the phenology of wild plants and crops1. However, the mechanisms by which plants sense temperature are not well understood. The evening complex is a major signalling hub and a core component of the plant circadian clock2,3. The evening complex acts as a temperature-responsive transcriptional repressor, providing rhythmicity and temperature responsiveness to growth through unknown mechanisms2,4–6. The evening complex consists of EARLY FLOWERING 3 (ELF3)4,7, a large scaffold protein and key component of temperature sensing; ELF4, a small α-helical protein; and LUX ARRYTHMO (LUX), a DNA-binding protein required to recruit the evening complex to transcriptional targets. ELF3 contains a polyglutamine (polyQ) repeat8–10, embedded within a predicted prion domain (PrD). Here we find that the length of the polyQ repeat correlates with thermal responsiveness. We show that ELF3 proteins in plants from hotter climates, with no detectable PrD, are active at high temperatures, and lack thermal responsiveness. The temperature sensitivity of ELF3 is also modulated by the levels of ELF4, indicating that ELF4 can stabilize the function of ELF3. In both Arabidopsis and a heterologous system, ELF3 fused with green fluorescent protein forms speckles within minutes in response to higher temperatures, in a PrD-dependent manner. A purified fragment encompassing the ELF3 PrD reversibly forms liquid droplets in response to increasing temperatures in vitro, indicating that these properties reflect a direct biophysical response conferred by the PrD. The ability of temperature to rapidly shift ELF3 between active and inactive states via phase transition represents a previously unknown thermosensory mechanism.

Suggested Citation

  • Jae-Hoon Jung & Antonio D. Barbosa & Stephanie Hutin & Janet R. Kumita & Mingjun Gao & Dorothee Derwort & Catarina S. Silva & Xuelei Lai & Elodie Pierre & Feng Geng & Sol-Bi Kim & Sujeong Baek & Chloe, 2020. "A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis," Nature, Nature, vol. 585(7824), pages 256-260, September.
  • Handle: RePEc:nat:nature:v:585:y:2020:i:7824:d:10.1038_s41586-020-2644-7
    DOI: 10.1038/s41586-020-2644-7
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    Citations

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    Cited by:

    1. Shuai Sun & Zhiqiang Liu & Xiaotian Wang & Jia Song & Siyu Fang & Jisheng Kong & Ren Li & Huanzhong Wang & Xia Cui, 2024. "Genetic control of thermomorphogenesis in tomato inflorescences," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    2. Tuo Ji & Lihua Zheng & Jiale Wu & Mei Duan & Qianwen Liu & Peng Liu & Chen Shen & Jinling Liu & Qinyi Ye & Jiangqi Wen & Jiangli Dong & Tao Wang, 2023. "The thioesterase APT1 is a bidirectional-adjustment redox sensor," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Huaijun Wang & Tiantian Ye & Zilong Guo & Yilong Yao & Haifu Tu & Pengfei Wang & Yu Zhang & Yao Wang & Xiaokai Li & Bingchen Li & Haiyan Xiong & Xuelei Lai & Lizhong Xiong, 2024. "A double-stranded RNA binding protein enhances drought resistance via protein phase separation in rice," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    4. Yong Ryoul Kim & Jaegeon Joo & Hee Jung Lee & Chaelim Kim & Ju-Chan Park & Young Suk Yu & Chang Rok Kim & Do Hui Lee & Joowon Cha & Hyemin Kwon & Kimberley M. Hanssen & Thomas G. P. Grünewald & Murim , 2024. "Prion-like domain mediated phase separation of ARID1A promotes oncogenic potential of Ewing’s sarcoma," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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