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URM1-Mediated Ubiquitin-Like Modification Is Required for Oxidative Stress Adaptation During Infection of the Rice Blast Fungus.

Identifieur interne : 000184 ( Main/Exploration ); précédent : 000183; suivant : 000185

URM1-Mediated Ubiquitin-Like Modification Is Required for Oxidative Stress Adaptation During Infection of the Rice Blast Fungus.

Auteurs : Luyang Wang [République populaire de Chine] ; Xuan Cai [République populaire de Chine] ; Junjie Xing [République populaire de Chine] ; Caiyun Liu [République populaire de Chine] ; Ahmed Hendy [République populaire de Chine, Égypte] ; Xiao-Lin Chen [République populaire de Chine]

Source :

RBID : pubmed:31551975

Abstract

Ubiquitin is a small modifier protein which is usually conjugated to substrate proteins for degradation. In recent years, a number of ubiquitin-like proteins have been identified; however, their roles in eukaryotes are largely unknown. Here, we describe a ubiquitin-like protein URM1, and found it plays important roles in the development and infection process of the rice blast fungus, Magnaporthe oryzae. Targeted deletion of URM1 in M. oryzae resulted in slight reduction in vegetative growth and significant decrease in conidiation. More importantly, the Δurm1 mutant also showed evident reduction in virulence to host plants. Infection process observation demonstrated that the mutant was arrested in invasive growth and resulted in accumulation of massive host reactive oxygen species (ROS). Further, we found the Δurm1 mutant was sensitive to the cell wall disturbing reagents, thiol oxidizing agent diamide and rapamycin. We also showed that URM1-mediated modification was responsive to oxidative stresses, and the thioredoxin peroxidase Ahp1 was one of the important urmylation targets. These results suggested that URM1-mediated urmylation plays important roles in detoxification of host oxidative stress to facilitate invasive growth in M. oryzae.

DOI: 10.3389/fmicb.2019.02039
PubMed: 31551975
PubMed Central: PMC6746893


Affiliations:


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<div type="abstract" xml:lang="en">Ubiquitin is a small modifier protein which is usually conjugated to substrate proteins for degradation. In recent years, a number of ubiquitin-like proteins have been identified; however, their roles in eukaryotes are largely unknown. Here, we describe a ubiquitin-like protein URM1, and found it plays important roles in the development and infection process of the rice blast fungus,
<i>Magnaporthe oryzae</i>
. Targeted deletion of
<i>URM1</i>
in
<i>M. oryzae</i>
resulted in slight reduction in vegetative growth and significant decrease in conidiation. More importantly, the Δ
<i>urm1</i>
mutant also showed evident reduction in virulence to host plants. Infection process observation demonstrated that the mutant was arrested in invasive growth and resulted in accumulation of massive host reactive oxygen species (ROS). Further, we found the Δ
<i>urm1</i>
mutant was sensitive to the cell wall disturbing reagents, thiol oxidizing agent diamide and rapamycin. We also showed that URM1-mediated modification was responsive to oxidative stresses, and the thioredoxin peroxidase Ahp1 was one of the important urmylation targets. These results suggested that URM1-mediated urmylation plays important roles in detoxification of host oxidative stress to facilitate invasive growth in
<i>M. oryzae</i>
.</div>
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<i>Magnaporthe oryzae</i>
. Targeted deletion of
<i>URM1</i>
in
<i>M. oryzae</i>
resulted in slight reduction in vegetative growth and significant decrease in conidiation. More importantly, the Δ
<i>urm1</i>
mutant also showed evident reduction in virulence to host plants. Infection process observation demonstrated that the mutant was arrested in invasive growth and resulted in accumulation of massive host reactive oxygen species (ROS). Further, we found the Δ
<i>urm1</i>
mutant was sensitive to the cell wall disturbing reagents, thiol oxidizing agent diamide and rapamycin. We also showed that URM1-mediated modification was responsive to oxidative stresses, and the thioredoxin peroxidase Ahp1 was one of the important urmylation targets. These results suggested that URM1-mediated urmylation plays important roles in detoxification of host oxidative stress to facilitate invasive growth in
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