Source: [Science Network] The Rice E3 ubiquitin ligase library was used to identify the key protein OsFBK16, which degrades OsPALs and regulates rice blast resistance. Photo provided by the Chinese Academy of Agricultural Sciences Recently, the innovative team of the functional g

Source: [Science Network]

uses the rice E3 ubiquitin ligase library to identify the key protein OsFBK16 that degrades OsPALs and regulates resistance to rice blast disease. Photo provided by of the Chinese Academy of Agricultural Sciences

Recently, the innovative team of functional genome research on crop pathogens in the Institute of Plant Protection, Chinese Academy of Agricultural Sciences Crop Pathogens published a research paper in Genome Biology. This study created the first E3 ubiquitin ligase (UbE3) library in plants for the identification of ubiquitin interaction group, and used this library to identify the core E3 ubiquitin ligase OsFBK16, a phenylalanase family protein PALs, revealing the molecular mechanism by which OsFBK16 negatively regulates rice blast resistance.

ubiquitination modification is one of the most important post-translation modifications of protein in eukaryotic organisms. It plays a key role in protein degradation, cell cycle regulation, transcription regulation and signal transduction. Identification of E3 ubiquitin ligase and its ubiquitinated substrate is the focus and difficulty of ubiquitination modification research. Studies in the past decade have shown that a large number of ubiquitinated proteins have been identified in animals and plants by using monoclonal antibodies that specifically recognize ubiquitinated sites. However, due to the lack of a systematic E3 ubiquitin ligase identification system, the corresponding E3 ubiquitin ligases of most ubiquitinated proteins are not clear.

In order to create an efficient E3 ubiquitin ligase identification system, the study systematically analyzed 1,515 E3 ubiquitin ligase genes (accounting for 4.73% of the total rice genes). 1499 full-length coding sequences of E3 ubiquitin ligases were obtained by PCR amplification and large-scale gene synthesis (covering 98.94% of ubiquitin ligase) and a homogeneous rice E3 ubiquitin ligase yeast library (UbE3 library) was created.

To verify the effectiveness of the UbE3 library, the study first screened the key ubiquitinated proteins that have been reported to be involved in biological processes such as rice drought, high salt and disease resistance, respectively. The results show that the UbE3 library can efficiently identify reported and novel E3 ubiquitin ligases.

The UbE3 library constructed by this study is the first complete E3 ubiquitin ligase library in plants. It provides powerful proteomic resources and lays an important foundation for the construction of the "E3 ubiquitin ligase-ubiquitinated protein" interaction group. Due to the importance and conservatism of ubiquitination modification in eukaryotes, this library also has important reference and application value for other species.

Associate Researcher Wang Ruyi from the Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Dr. You Xiaoman, Dr. Zhang Chongyang and Dr. Fang Hong are the co-first authors of the paper, and Researcher Joseph Ning is the corresponding author of the paper . Institute of Genetics and Developmental Biology, Chinese Academy of Sciences Researcher Xie Qi and others participated in the research of this project. The research was funded by projects such as National Natural Science Foundation of China and Innovation Engineering of Chinese Academy of Agricultural Sciences.

Related paper information: https://doi.org/10.1007/s00122-022-04139-3

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