Signals in hepatitis A virus P3 region proteins recognized by the ubiquitin-mediated proteolytic system
Signals in hepatitis A virus P3 region proteins recognized by the ubiquitin-mediated proteolytic system
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DOI：
10.1016/s0042-6822(03)00071-0
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发表时间：
2003-05-10
期刊：
影响因子：
3.7
通讯作者：
Lawson, TG
中科院分区：
文献类型：
--
作者：
Losick, VP;Schlax, PE;Lawson, TG
甲型肝炎病毒3C蛋白酶和3D RNA聚合酶在感染细胞中以低浓度存在。3C蛋白酶以前被证明可以被泛素/26S蛋白酶体系统快速降解，我们在这里提供的证据表明，3D聚合酶也受到泛素化介导的蛋白水解的影响。我们的研究结果表明，3C蛋白酶中的序列（32）LGVKDDWLLV（41）可作为泛素蛋白连接酶e3α识别的蛋白质破坏信号，而RNA聚合酶的破坏信号不需要羧基端137个氨基酸。病毒3ABCD多蛋白和3CD二蛋白也被发现是泛素介导的蛋白水解的底物。试图确定3C蛋白酶或3D聚合酶破坏信号是否触发这些前体的泛素化和降解，得到的证据表明，但不能明确证明，泛素系统对3D聚合酶的识别是负责的。(C) 2003 Elsevier Science（美国）版权所有。
The hepatitis A virus 3C protease and 3D RNA polymerase are present in low concentrations in infected cells. The 3C protease was previously shown to be rapidly degraded by the ubiquitin/26S proteasome system and we present evidence here that the 3D polymerase is also subject to ubiquitination-mediated proteolysis. Our results show that the sequence (32)LGVKDDWLLV(41) in the 3C protease serves as a protein destruction signal recognized by the ubiquitin-protein ligase E3alpha and that the destruction signal for the RNA polymerase does not require the carboxyl-terminal 137 amino acids. Both the viral 3ABCD polyprotein and the 3CD diprotein were also found to be substrates for ubiquitin-mediated proteolysis. Attempts to determine if the 3C protease or the 3D polymerase destruction signals trigger the ubiquitination and degradation of these precursors yielded evidence suggesting, but not unequivocally proving, that the recognition of the 3D polymerase by the ubiquitin system is responsible. (C) 2003 Elsevier Science (USA). All rights reserved.