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

Chuanyang Yu, Stephen King Pong Leung, Wenxin Zhang, Louis Tung Faat Lai, Ying Ki Chan, Man Chit Wong, Samir Benlekbir, Yong Cui, Liwen Jiang and Wilson Chun Yu Lau ()
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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
Wilson Chun Yu Lau: The Chinese University of Hong Kong, Shatin

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-23338-y

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