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The farnesyltransferase beta-subunit RAM1 regulates localization of RAS proteins and appressorium-mediated infection in Magnaporthe oryzae

文献类型： 外文期刊

作者： Hendy, Ahmed Aboelfotoh 3 ; Xing, Junjie 2 ; Chen, Xiaoyang 1 ; Chen, Xiao-Lin 1 ;

作者机构： 1.Huazhong Agr Univ, Coll Plant Sci & Technol, Prov Key Lab Plant Pathol Hubei Prov, Wuhan 430070, Hubei, Peoples R China

2.Hunan Hybrid Rice Res Ctr, State Key Lab Hybrid Rice, Changsha 410125, Hunan, Peoples R China

3.Alexandria Univ, Fac Agr Saba Basha, Dept Agr Bot, Alexandria 21531, Egypt

关键词： appressorium formation; cAMP signalling pathway; farnesylation; RAS protein; rice blast fungus

期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：5.663； 五年影响因子：5.626 ）

ISSN： 1464-6722

年卷期：

页码：

收录情况： SCI

摘要： Post-translational farnesylation can regulate subcellular localization and protein-protein interaction in eukaryotes. The function of farnesylation is not well identified in plant pathogenic fungi, particularly during the process of fungal infection. Here, through functional analyses of the farnesyltransferase beta-subunit gene, RAM1, we examine the importance of protein farnesylation in the rice blast fungus Magnaporthe oryzae. Targeted disruption of RAM1 resulted in the reduction of hyphal growth and sporulation, and an increase in the sensitivity to various stresses. Importantly, loss of RAM1 also led to the attenuation of virulence on the plant host, characterized by decreased appressorium formation and invasive growth. Interestingly, the defect in appressoria formation of the Delta ram1 mutant can be recovered by adding exogenous cAMP and IBMX, suggesting that RAM1 functions upstream of the cAMP signalling pathway. We found that two Ras GTPases, RAS1 and RAS2, can interact with Ram1, and their plasma membrane localization was regulated by Ram1 through their C-terminal farnesylation sites. Adding a farnesyltransferase inhibitor Tipifarnib can result in similar defects as in Delta ram1 mutant, including decreased appressorium formation and invasive growth, as well as mislocalized RAS proteins. Our findings indicate that protein farnesylation regulates the RAS protein-mediated signaling pathways required for appressorium formation and host infection, and suggest that abolishing farnesyltransferase could be an effective strategy for disease control.

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