Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein.

Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein.
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DOI:
10.1016/j.virol.2009.11.010
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发表时间:
2010-02-20
期刊:
影响因子:
3.7
通讯作者:
Nagy PD
Nagy PD
中科院分区:
医学3区
文献类型:
--
作者:
Barajas D;Nagy PD

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病毒复制蛋白的翻译后修饰可能是正链RNA病毒复制过程中的普遍现象。在本文中,我们鉴定了参与泛素化的番茄病毒p33复制辅助因子中的两个赖氨酸,并表明相同的赖氨酸对p33与宿主Vps23p ESCRT-I因子的相互作用也是重要的。我们发现,p33与Vps23p的相互作用也受到p33中类似“晚期结构域”的序列的影响。P33中两个赖氨酸和晚期结构域样序列的组合突变降低了番茄丛矮病毒复制子RNA在酵母模型宿主、植物原生质体和植物叶片中的复制,表明p33-Vps23p ESCRT蛋白相互作用影响番茄病毒的复制。使用泛素模拟p33嵌合体,我们证明了高水平的p33泛素化对TBSV复制具有抑制作用。这些发现认为,p33泛素化的最佳水平在番茄病毒感染过程中起着调节作用。
Post-translational modifications of viral replication proteins could be widespread phenomena during the replication of plus-stranded RNA viruses. In this paper, we identify two lysines in the tombusvirus p33 replication co-factor involved in ubiquitination and show that the same lysines are also important for the p33 to interact with the host Vps23p ESCRT-I factor. We find that the interaction of p33 with Vps23p is also affected by a "late-domain"-like sequence in p33. The combined mutations of the two lysines and the late-domain-like sequences in p33 reduced replication of a replicon RNA of Tomato bushy stunt virus in yeast model host, in plant protoplasts and plant leaves, suggesting that p33-Vps23p ESCRT protein interaction affects tombusvirus replication. Using ubiquitin-mimicking p33 chimeras, we demonstrate that high level of p33 ubiquitination is inhibitory for TBSV replication. These findings argue that optimal level of p33 ubiquitination plays a regulatory role during tombusvirus infections.
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发表时间: 2009-03-01
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