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Structural basis of substrate recognition and thermal protection by a small heat shock protein

Author

Listed:
  • Chuanyang Yu

    (The Chinese University of Hong Kong, Shatin)

  • Stephen King Pong Leung

    (The Chinese University of Hong Kong, Shatin)

  • Wenxin Zhang

    (The Chinese University of Hong Kong, Shatin)

  • Louis Tung Faat Lai

    (The Chinese University of Hong Kong, Shatin)

  • Ying Ki Chan

    (The Chinese University of Hong Kong, Shatin)

  • Man Chit Wong

    (The Chinese University of Hong Kong, Shatin)

  • Samir Benlekbir

    (The Hospital for Sick Children Research Institute)

  • Yong Cui

    (Xiamen University)

  • Liwen Jiang

    (The Chinese University of Hong Kong, Shatin
    The Chinese University of Hong Kong, Shatin
    The Chinese University of Hong Kong)

  • Wilson Chun Yu Lau

    (The Chinese University of Hong Kong, Shatin)

Abstract

Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp-substrate complexes has been hampered by the transient and heterogeneous nature of their interactions, and the precise mechanisms underlying substrate recognition, promiscuity, and chaperone activity of sHsps remain unclear. Here we show the formation of a stable complex between Arabidopsis thaliana plastid sHsp, Hsp21, and its natural substrate 1-deoxy-D-xylulose 5-phosphate synthase (DXPS) under heat stress, and report cryo-electron microscopy structures of Hsp21, DXPS and Hsp21-DXPS complex at near-atomic resolution. Monomeric Hsp21 binds across the dimer interface of DXPS and engages in multivalent interactions by recognizing highly dynamic structural elements in DXPS. Hsp21 partly unfolds its central α-crystallin domain to facilitate binding of DXPS, which preserves a native-like structure. This mode of interaction suggests a mechanism of sHsps anti-aggregation activity towards a broad range of substrates.

Suggested Citation

  • Chuanyang Yu & Stephen King Pong Leung & Wenxin Zhang & Louis Tung Faat Lai & Ying Ki Chan & Man Chit Wong & Samir Benlekbir & Yong Cui & Liwen Jiang & Wilson Chun Yu Lau, 2021. "Structural basis of substrate recognition and thermal protection by a small heat shock protein," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23338-y
    DOI: 10.1038/s41467-021-23338-y
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    Cited by:

    1. Yao-Xu Mao & Zhi-Peng Chen & Liang Wang & Jie Wang & Cong-Zhao Zhou & Wen-Tao Hou & Yuxing Chen, 2024. "Transport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Zhi-Peng Chen & Da Xu & Liang Wang & Yao-Xu Mao & Yang Li & Meng-Ting Cheng & Cong-Zhao Zhou & Wen-Tao Hou & Yuxing Chen, 2022. "Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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