N-terminal acetylation of the βC1 protein encoded by the betasatellite of tomato yellow leaf curl China virus is critical for its viral pathogenicity.
N-terminal acetylation of the βC1 protein encoded by the betasatellite of tomato yellow leaf curl China virus is critical for its viral pathogenicity.
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DOI：
10.1016/j.virol.2023.07.003
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发表时间：
2023-07
期刊：
影响因子：
3.7
通讯作者：
Yaqin Wang;Tao Hu;Yuting He;Chenlu Su;Zhanqi Wang;Xueping Zhou
中科院分区：
文献类型：
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作者：
Yaqin Wang;Tao Hu;Yuting He;Chenlu Su;Zhanqi Wang;Xueping Zhou
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 aboutN-acetylation of viral proteins. Here, we identified the Thr residue at position 2 (Thr-2) in the βC1 protein encoded by the betasatellite of tomato yellow leaf curl China virus (TYLCCNB-βC1) as a novelN-acetylation site. Furthermore, the effects of TYLCCNB-βC1N-acetylation on its function as a pathogenicity factor were determined viaN-acetylation mutants in Nicotiana benthamiana plants. We found thatN-acetylation of TYLCCNB-βC1 is critical for its self-interaction in the nucleus and viral pathogenesis, and that removal ofN-acetylation of TYLCCNB-βC1 attenuated tomato yellow leaf curl China virus-induced symptoms and led to accelerated degradation of TYLCCNB-βC1 through the ubiquitin-proteasome system. Our data reveal a protective effect ofN-acetylation of TYLCCNB-βC1 on its pathogenesis and demonstrate an antagonistic crosstalk betweenN-acetylation and ubiquitination in this geminiviral protein.
