N-terminal acetylation of the & beta;C1 protein encoded by the betasatellite of tomato yellow leaf curl China virus is critical for its viral pathogenicity

文献类型： 外文期刊

第一作者： Wang, Yaqin

作者： Wang, Yaqin;Hu, Tao;He, Yuting;Su, Chenlu;Zhou, Xueping;Wang, Zhanqi;Zhou, Xueping;Zhou, Xueping

作者机构：

关键词： Pathogenesis; N-Acetylation; Ubiquitination; Ubiquitin-proteasome system

期刊名称：VIROLOGY （ 影响因子：3.7； 五年影响因子：3.2 ）

ISSN： 0042-6822

年卷期： 2023 年 586 卷

页码：

收录情况： SCI

摘要： N-terminal acetylation (N-acetylation) is one of the most common protein modifications and plays crucial roles in viability and stress responses in animals and plants. However, very little is known about N-acetylation of viral proteins. Here, we identified the Thr residue at position 2 (Thr-2) in the I3C1 protein encoded by the betasatellite of tomato yellow leaf curl China virus (TYLCCNB-I3C1) as a novel N-acetylation site. Furthermore, the effects of TYLCCNB-I3C1 N-acetylation on its function as a pathogenicity factor were determined via N-acetylation mutants in Nicotiana benthamiana plants. We found that N-acetylation of TYLCCNB-I3C1 is critical for its self-interaction in the nucleus and viral pathogenesis, and that removal of N-acetylation of TYLCCNB-I3C1 attenuated tomato yellow leaf curl China virus-induced symptoms and led to accelerated degradation of TYLCCNB-I3C1 through the ubiquitin-proteasome system. Our data reveal a protective effect of N-acetylation of TYLCCNB-I3C1 on its pathogenesis and demonstrate an antagonistic crosstalk between N-acetylation and ubiquitination in this gem-iniviral protein.

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