Structural basis for Ca2+-dependent activation of a plant metacaspase

Ping Zhu, Xiao-Hong Yu, Cheng Wang, Qingfang Zhang, Wu Liu, Sean McSweeney, John Shanklin (), Eric Lam () and Qun Liu ()
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Ping Zhu: Brookhaven National Laboratory
Xiao-Hong Yu: Brookhaven National Laboratory
Cheng Wang: Brookhaven National Laboratory
Qingfang Zhang: Brookhaven National Laboratory
Wu Liu: Brookhaven National Laboratory
Sean McSweeney: Brookhaven National Laboratory
John Shanklin: Brookhaven National Laboratory
Eric Lam: The State University of New Jersey
Qun Liu: Brookhaven National Laboratory

Nature Communications, 2020, vol. 11, issue 1, 1-9

Abstract: Abstract Plant metacaspases mediate programmed cell death in development, biotic and abiotic stresses, damage-induced immune response, and resistance to pathogen attack. Most metacaspases require Ca2+ for their activation and substrate processing. However, the Ca2+-dependent activation mechanism remains elusive. Here we report the crystal structures of Metacaspase 4 from Arabidopsis thaliana (AtMC4) that modulates Ca2+-dependent, damage-induced plant immune defense. The AtMC4 structure exhibits an inhibitory conformation in which a large linker domain blocks activation and substrate access. In addition, the side chain of Lys225 in the linker domain blocks the active site by sitting directly between two catalytic residues. We show that the activation of AtMC4 and cleavage of its physiological substrate involve multiple cleavages in the linker domain upon activation by Ca2+. Our analysis provides insight into the Ca2+-dependent activation of AtMC4 and lays the basis for tuning its activity in response to stresses for engineering of more sustainable crops for food and biofuels.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15830-8

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DOI: 10.1038/s41467-020-15830-8

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