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

Author

Listed:
  • Joon-Yung Cha

    (Gyeongsang National University)

  • Jeongsik Kim

    (The Ohio State University
    Institute for Basic Science (IBS))

  • Tae-Sung Kim

    (The Ohio State University
    Korea National Open University)

  • Qingning Zeng

    (The Ohio State University)

  • Lei Wang

    (The Ohio State University
    Institute of Botany, Chinese Academy of Sciences)

  • Sang Yeol Lee

    (Gyeongsang National University)

  • Woe-Yeon Kim

    (Gyeongsang National University)

  • David E. Somers

    (The Ohio State University)

Abstract

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.

Suggested Citation

  • Joon-Yung Cha & Jeongsik Kim & Tae-Sung Kim & Qingning Zeng & Lei Wang & Sang Yeol Lee & Woe-Yeon Kim & David E. Somers, 2017. "GIGANTEA is a co-chaperone which facilitates maturation of ZEITLUPE in the Arabidopsis circadian clock," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-016-0014-9
    DOI: 10.1038/s41467-016-0014-9
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