PARylation of 14-3-3 Proteins Controls the Virulence of Magnaporthe Oryzae

Overview

Journal Nat Commun

Specialty Biology

Date 2024 Sep 14

PMID 39277621

Authors

Xiuqin Gao

Gaigai Gao

Weifeng Zheng

Haibing Liu

Wenbo Pan

Xi Xia

Dongmei Zhang

Wenwei Lin

Zonghua Wang

Baomin Feng

Affiliations

Soon will be listed here.

Abstract

Magnaporthe oryzae is a devastating fungal pathogen that causes the rice blast disease worldwide. The post-translational modification of ADP-ribosylation holds significant importance in various fundamental biological processes. However, the specific function of this modification in M. oryzae remains unknown. This study revealed that Poly(ADP-ribosyl)ation (PARylation) executes a critical function in M. oryzae. M. oryzae Poly(ADP-ribose) polymerase 1 (PARP1) exhibits robust PARylation activity. Disruption of PARylation by PARP1 knock-out or chemical inhibition reveals its involvement in M. oryzae virulence, particularly in appressorium formation. Furthermore, we identified two M. oryzae 14-3-3 proteins, GRF1 and GRF2, as substrates of PARP1. Deletion of GRF1 or GRF2 results in delayed and dysfunctional appressorium, diminished plant penetration, and reduced virulence of the fungus. Biochemical and genetic evidence suggest that PARylation of 14-3-3s is essential for its function in M. oryzae virulence. Moreover, PARylation regulates 14-3-3 dimerization and is required for the activation of the mitogen-activated protein kinases (MAPKs), Pmk1 and Mps1. GRF1 interacts with both Mst7 and Pmk1, and bridges their interaction in a PARylation-dependent manner. This study unveils a distinctive mechanism that PARylation of 14-3-3 proteins controls appressorium formation through MAPK activation, and could facilitate the development of new strategies of rice blast disease control.

Citing Articles

Poly ADP-Ribosylation in a Plant Pathogenic Oomycete : A Key Controller of Growth and Host Plant Colonisation.

Samarskaya V, Koblova S, Suprunova T, Rogozhin E, Spechenkova N, Yakunina S J Fungi (Basel). 2025; 11(1).

PMID: 39852448 PMC: 11766942. DOI: 10.3390/jof11010029.

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