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Global analysis of sumoylation function reveals novel insights into development and appressorium‐mediated infection of the rice blast fungus
Author(s) -
Liu Caiyun,
Li Zhigang,
Xing Junjie,
Yang Jun,
Wang Zhao,
Zhang Hong,
Chen Deng,
Peng YouLiang,
Chen XiaoLin
Publication year - 2018
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.15141
Subject(s) - sumo protein , appressorium , biology , septin , microbiology and biotechnology , virulence , effector , magnaporthe , mutant , genetics , ubiquitin , cytokinesis , conidium , magnaporthe grisea , gene , cell division , oryza sativa , cell
Summary Protein post‐translational modifications play critical roles in cellular processes, development and stress response. The small ubiquitin‐like modifier ( SUMO ) to proteins is one of the essential modifications in eukaryotes, but its function remains largely unknown in plant pathogenic fungi. We present a comprehensive analysis combined with proteomic, molecular and cellular approaches to explore the roles of sumoylation in the model plant fungal pathogen, Magnaporthe oryzae . We found the SUMO pathway plays key roles in colony growth, conidia formation and virulence to the host, as well as cell‐cycle‐related phenotypes. Sumoylation is also involved in responding to different stresses. Affinity purification identified 940 putative SUMO substrates, many of which were reported to be involved in development, stress response and infection. Interestingly, four septins were also shown to be sumoylated. Mutation of consensus sumoylation sites in each septin all resulted in reduced virulence to the host and dislocation of septins in appressoria. Moreover, sumoylation is also involved in extracellular secretion of different effector proteins. Our study on the functions of sumoylation provides novel insight into development and infection of the rice blast fungus.