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

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Zhu P,Yu XH,Wang C,Zhang Q,Liu W,McSweeney S,Shanklin J,Lam E,Liu Q

doi

10.1038/s41467-020-15830-8

subject

Has Abstract

pub_date

2020-05-07 00:00:00

pages

2249

issue

1

issn

2041-1723

pii

10.1038/s41467-020-15830-8

journal_volume

11

pub_type

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