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中国植物病理学会第十一届全国会员代表大会暨2018年学...

作者： Zheng Huawei Li Lingping Miao Pengfei Wu Congxian Chen Xiaomin Yuan Mingyue Fang Tian Justice Norvienyeku Li Guangpu Zheng Wenhui Wang Zonghua Zhou Jie State Key Laboratory of Ecological Pest Control for Fujian and Taiwan Crops College of Plant ProtectionFujian Agriculture and Forestry University Fujian Province Key Laboratory of Pathogenic Fungi and Mycotoxins College of Life SciencesFujian Agriculture and Forestry University College of Ocean Science Minjiang University

Sec4/Rab8 is one of the well-studied members of the Rab GTPase family,findings have shown that Sec4/Rab8 crucially promotes the pathogenesis of phytopathogens,but the up stream regulators of Rab8 are still unknown.Here,we identify two Sec2 homologs FgSec2A and FgSec2B in devastating fungal pathogen Fusarium graminearum,and investigate their role and relationship with FgRab8 by live-cell imaging,genetic and functional analyses.Yeast two-hybrid assay shows that FgSec2A specifically interacts with FgRab8 DN（N123I） and itself.Importantly,FgSec2A is required for growth,conidiation,DON production,and virulence of F.graminearum.Live-cell imaging shows that FgSec2A and FgSec2B are localized at the tip region of hyphae and conidia.Both N-terminal region and Sec2 domain of FgSec2A are essential for its function,but not for localization,while the C-terminal region is important for its polarized localization.Constitutively active FgRab8 CA（Q69L） partially rescue defects exhibited by the ΔFgsec2A strain.Consistently,FgSec2A is required for the polarized localization of FgRab8.Furthermore,FgSec2A and FgSec2B have redundant functions,but FgSec2A not interact and colocalize with FgSec2B.Taken together,these results indicate that FgSec2A acts as a FgRab8 guanine nucleotide exchange factor and is required for polarized growth,DON production and pathogenicity in F.graminearum.

关键词： FgSec2 guanine nucleotide exchange factor Sec4/Rab8 DON Pathogenicity Fusarium graminearum

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Phosphorylation of MtRopGEF2 by LYK3 mediates MtROP activity to regulate rhizobial infection in Medicago truncatula

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Journal of Integrative Plant Biology 2021年第10期63卷 1787-1800页

作者： Mingxing Wang Huan Feng Peng Xu Qiujin Xie Jinpeng Gao Yanzhang Wang Xiaowei Zhang Jun Yang Jeremy DMurray Fengli Sun Chunyan Wang Ertao Wang Nan Yu College of Life and Environment Sciences Shanghai Normal UniversityShanghai 200234China National key Laboratory of Plant Molecular Genetics Center for Excellence in Molecular Plant SciencesInstitute of Plant Physiology and Ecologythe Chinese Academy of SciencesShanghai 200032China University of Chinese Academy of Sciences Beijing 100039China College of Forestry Northwest A&F UniversityYangling 712100China College of Agronomy Northwest A&F UniversityYangling 712100China

The formation of nitrogen-fixing no dules on legume roots requires the coordination of infection by rhizobia at the root epidermis with the initiation of cell divisions in the root cortex.During infection,rhizobia attach to the tip of elongating root hairs which then curl to entrap the rhizobia.However,the mechanism of root hair deformation and curling in response to symbiotic signals is still elusive.Here,we found that small GTPases(MtRac1/MtROP9 and its homologs)are required for root hair development and rhizobial infection in Medicago truncatula.Our results show that the Nod factor receptor LYK3 phosphorylates the guanine nucleotide exchange factor MtRopGEF2 at S73 which is critical for the polar growth of root hairs.In turn,phosphorylated MtRopGEF2 can activate MtRac1.Activated MtRac1 was found to localize at the tips of root hairs and to strongly interact with LYK3 and NFP.Taken together,our results support the hypothesis that MtRac1,LYK3,and NFP form a polarly localized receptor complex that regulates root hair deformation during rhizobial infection.

关键词： guanine nucleotide exchange factor ROP GTPase root hair deformation rhizobial infection

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维普期刊数据库

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Structure and Expression of Several Putative Cdc42-Interacting Proteins in Magnaporthe grisea

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Agricultural Sciences in China 2006年第10期5卷 780-786页

作者： ZHENG Wu CHEN Ji-sheng ZHENG Shi-qin LU Guo-dong WANG Zong-hua Key Laboratory of Bio-pesticide and Chemistry Biology Ministry of Education/Functional Genomics Center Fujian Agriculture and Forestry University Fuzhou 350002 P.R.China

MgCdc42 （Cdc42 in Magnaporthe grisea）, with high homology to ScCdc42 （Cdc42 in Saccharomyces cerevisiae）, has been demonstrated to involve in the morphogenesis and infection process. To further understand the signaling network, the putative MgCdc42-interacting proteins were analyzed. ScCdc42-interacting protein sequences were first used to BLAST against the M. grisea genome database to retrieve their corresponding analogs. Subsequently, conserved domains of these proteins were compared and expression patterns of their encoding genes in different MgCdc42 mutation states were analyzed by semiquantitative RT-PCR. All retrieved analogs of ScCdc42-interacting proteins from the M. grisea database have conserved domains as those in S. cerevisiae. Expression of their encoding genes increased in MgCdc42CA mutant and decreased in MgCdc42KO mutant. However, MgBeml, Chin1, and MgGicl in MgCdc42DN mutant had the same expression level as that in the wild type, although MgBem4, MgBoi2, MgCdc24, MgGic2, MgRgal, and Mst20 had decreased expression level, as expected. Overall, it is concluded that there may exist a similar Cdc42 signal pathway in M. grisea as in S. cerevisiae and MgCdc42 plays a key role in the pathway.

关键词： Cdc42 Magnaporthe grisea guanine nucleotide exchange factor GTPase-activating protein

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