期刊论文详细信息
PLoS Pathogens
Eight RGS and RGS-like Proteins Orchestrate Growth, Differentiation, and Pathogenicity of Magnaporthe oryzae
Ping Wang1  Zhongqiang Qi2  Qian Huang2  Xin Zhang2  Haifeng Zhang2  Jiansheng Wang2  Kaiyue Liu2  Wei Tang2  Xiaobo Zheng2  Yue Chen2  Zhengguang Zhang2  Zhengyi Wang3  Xia Yan3 
[1] Department of Pediatrics and the Research Institute for Children, Louisiana State University Health Sciences Center, New Orleans, Louisiana, United States of America;Department of Plant Pathology, College of Plant Protection, Nanjing Agricultural University, and Key Laboratory of Integrated Management of Crop Diseases and Pests, Ministry of Education, Nanjing, China;State Key Laboratory for Rice Biology, Biotechnology Institute, Zhejiang University, Huajiachi Campus, Hangzhou, China
关键词: Appressoria;    G-protein signaling;    Pathogenesis;    Mutant strains;    Fungal pathogens;    Laccases;    Rice blast fungus;    Peroxidases;   
DOI  :  10.1371/journal.ppat.1002450
学科分类:生物科学(综合)
来源: Public Library of Science
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【 摘 要 】

A previous study identified MoRgs1 as an RGS protein that negative regulates G-protein signaling to control developmental processes such as conidiation and appressorium formation in Magnaporthe oryzae. Here, we characterized additional seven RGS and RGS-like proteins (MoRgs2 through MoRgs8). We found that MoRgs1 and MoRgs4 positively regulate surface hydrophobicity, conidiation, and mating. Indifference to MoRgs1, MoRgs4 has a role in regulating laccase and peroxidase activities. MoRgs1, MoRgs2, MoRgs3, MoRgs4, MoRgs6, and MoRgs7 are important for germ tube growth and appressorium formation. Interestingly, MoRgs7 and MoRgs8 exhibit a unique domain structure in which the RGS domain is linked to a seven-transmembrane motif, a hallmark of G-protein coupled receptors (GPCRs). We have also shown that MoRgs1 regulates mating through negative regulation of Gα MoMagB and is involved in the maintenance of cell wall integrity. While all proteins appear to be involved in the control of intracellular cAMP levels, only MoRgs1, MoRgs3, MoRgs4, and MoRgs7 are required for full virulence. Taking together, in addition to MoRgs1 functions as a prominent RGS protein in M. oryzae, MoRgs4 and other RGS and RGS-like proteins are also involved in a complex process governing asexual/sexual development, appressorium formation, and pathogenicity.

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