The chloroplast ribosomal protein large subunit 1 interacts with viral polymerase and promotes virus infection.
The chloroplast ribosomal protein large subunit 1 interacts with viral polymerase and promotes virus infection.
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叶绿体核糖体蛋白大亚基1与病毒聚合酶相互作用促进病毒感染
DOI:
10.1093/plphys/kiab249
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发表时间:
2021-09-04
期刊:
影响因子:
7.4
通讯作者:
Li XD
中科院分区:
文献类型:
--
作者:
Cheng DJ;Xu XJ;Yan ZY;Tettey CK;Fang L;Yang GL;Geng C;Tian YP;Li XD
A chloroplast ribosomal protein competes with a host degradation factor to bind the viral RNA-dependent RNA polymerase and thus promotes tobacco vein banding mosaic virus infection. Chloroplasts play an indispensable role in the arms race between plant viruses and hosts. Chloroplast proteins are often recruited by plant viruses to support viral replication and movement. However, the mechanism by which chloroplast proteins regulate potyvirus infection remains largely unknown. In this study, we observed that Nicotiana benthamiana ribosomal protein large subunit 1 (NbRPL1), a chloroplast ribosomal protein, localized to the chloroplasts via its N-terminal 61 amino acids (transit peptide), and interacted with tobacco vein banding mosaic virus (TVBMV) nuclear inclusion protein b (NIb), an RNA-dependent RNA polymerase. Upon TVBMV infection, NbRPL1 was recruited into the 6K2-induced viral replication complexes in chloroplasts. Silencing of NbRPL1 expression reduced TVBMV replication. NbRPL1 competed with NbBeclin1 to bind NIb, and reduced the NbBeclin1-mediated degradation of NIb. Therefore, our results suggest that NbRPL1 interacts with NIb in the chloroplasts, reduces NbBeclin1-mediated NIb degradation, and enhances TVBMV infection.
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