한빛사 논문
Jinqiu Hea,1, Wenwu Yeb,1, Du Seok Choic,d,1, Baixing Wua, Yi Zhaic,d, Baodian Guob, Shuyi Duanb, Yuanchao Wangb, Jianhua Gane, Wenbo Mac,d,2, and Jinbiao Maa,2
a State Key Laboratory of Genetic Engineering, Ministry of Education Key Laboratory of Biodiversity Sciences and Ecological Engineering, Institute of Plant Biology, School of Life Sciences, Fudan University, 200438 Shanghai, China; b Department of Plant Pathology, Nanjing Agriculture University, 210095 Nanjing, China; c Department of Microbiology and Plant Pathology, University of California, Riverside, CA 92521; d Center for Plant Cell Biology, University of California, Riverside, CA 92521; and e State Key Laboratory of Genetic Engineering, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, 200438 Shanghai, China
1 J.H., W.Y., and D.S.C. contributed equally to this work.
2 To whom correspondence may be addressed.
Abstract
Phytophthora are eukaryotic pathogens that cause enormous losses in agriculture and forestry. Each Phytophthora species encodes hundreds of effector proteins that collectively have essential roles in manipulating host cellular processes and facilitating disease development. Here we report the crystal structure of the effector Phytophthora suppressor of RNA silencing 2 (PSR2). PSR2 produced by the soybean pathogen Phytophthora sojae (PsPSR2) consists of seven tandem repeat units, including one W-Y motif and six L-W-Y motifs. Each L-W-Y motif forms a highly conserved fold consisting of five α-helices. Adjacent units are connected through stable, directional linkages between an internal loop at the C terminus of one unit and a hydrophobic pocket at the N terminus of the following unit. This unique concatenation results in an overall stick-like structure of PsPSR2. Genome-wide analyses reveal 293 effectors from five Phytophthora species that have the PsPSR2-like arrangement, that is, containing a W-Y motif as the “start” unit, various numbers of L-W-Y motifs as the “middle” units, and a degenerate L-W-Y as the “end” unit. Residues involved in the interunit interactions show significant conservation, suggesting that these effectors also use the conserved concatenation mechanism. Furthermore, functional analysis demonstrates differential contributions of individual units to the virulence activity of PsPSR2. These findings suggest that the L-W-Y fold is a basic structural and functional module that may serve as a “building block” to accelerate effector evolution in Phytophthora.
microbial pathogenesis, effector evolution, tandem repeats, protein diversification, Phytophthora disease
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