The accumulation of the reactive oxygen species (ROS) in rice is important in its interaction with the rice blast fungus Magnaporthe oryzae during which the pathogen scavenges ROS through the production of extracellular enzymes that promote blast. We previously characterized the MoYvh1 protein phosphatase from M. oryzae that plays a role in scavenging of ROS. To understand the underlying mechanism, we found that MoYvh1 is translocated into the nucleus following oxidative stress and that this translocation is dependent on MoSsb1 and MoSsz1 that are homologous to heat-shock protein 70 (Hsp70) proteins. In addition, we established a link between MoYvh1 and MoMrt4, a ribosome maturation factor homolog whose function also involves shuttling between the cytoplasm and the nucleus. Moreover, we found that MoYvh1 regulates the production of extracellular proteins that modulate rice-immunity. Taking together, our evidence suggests that functions of MoYvh1 in regulating ROS scavenging require its nucleocytoplasmic shuttling and the partner proteins MoSsb1 and MoSsz1, as well as MoMrt4. Our findings provide novel insights into the mechanism by which M. oryzae responds to and subverts host immunity through the regulation of ribosome biogenesis and protein biosynthesis.
MoYvh1 subverts rice defense through functions of ribosomal protein MoMrt4 in Magnaporthe oryzae
Xinyu Liu,Jie Yang,Bin Qian,Yongchao Cai,Xiwen Zou,Haifeng Zhang,Xiaobo Zheng,Ping Wang,Zhengguang Zhang
Published 2018 in PLoS Pathogens
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- Publication year
2018
- Venue
PLoS Pathogens
- Publication date
2018-04-01
- Fields of study
Biology, Medicine, Chemistry, Environmental Science
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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