Phytophthora sojae effector Avr1d functions as an E2 competitor and inhibits ubiquitination activity of GmPUB13 to facilitate infection
Year: 2021
Type: article
Abstract: Significance Ubiquitination acts as a crucial regulator in plant immunity. Accordingly, microbial pathogens secrete effectors to hijack the host ubiquitination system. However, the molecular mechanisms by which effectors modulate the host ubiquitination system are not yet clear. Here, we found that the Phytophthora sojae effector Avr1d physically binds to the U-box-type E3 ligase GmPUB13, which proved to be a susceptibility factor. The crystal structure of Avr1d complexed with GmPUB13 revealed that Avr1d occupies the binding site in GmPUB13 for E2 ubiquitin conjugating enzyme and competes with E2 for binding to GmPUB13. Avr1d stabilized GmPUB13 by suppressing the self-ubiquitination activity of GmPUB13 and thereby promoting Phytophthora infection. This study reveals a structural basis for modulation of host targets by Phytophthora effectors.
Institutions: Nanjing Agricultural University, Chinese Academy of Sciences, Center for Excellence in Molecular Plant Sciences, University of Chinese Academy of Sciences, Huazhong Agricultural University, ShanghaiTech University, State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, China Agricultural University, Oregon State University, Shanghai Normal University
Language: English
Subfield: Plant Science
Domain: Life Sciences
SDG: Zero hunger
Open Access status: hybrid
OpenAlex ID: W3134055211