Ribosomal protein S5 interacts with the internal ribosomal entry site of hepatitis C virus
Ribosomal protein S5 interacts with the internal ribosomal entry site of hepatitis C virus
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DOI：
10.1074/jbc.c100206200
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发表时间：
2001-06-15
影响因子：
4.8
通讯作者：
Katayama, K
中科院分区：
文献类型：
--
作者：
Fukushi, S;Okada, M;Katayama, K
丙型肝炎病毒（HCV）基因组RNA的翻译起始发生在其高度结构化的5'非编码区，称为内部核糖体进入位点（IRES），最近的研究表明，HCV IRES和40s核糖体亚基形成了一个稳定的二元复合体，被认为对48s起始复合体的后续组装很重要。核糖体蛋白（rp） S9被认为是HCV IRES与40s亚基结合的主要候选蛋白。在紫外交联实验中，RpS9的分子质量约为25 kDa。在本研究中，我们检测了40s核糖体中与HCV IRES在UV交联后形成复合物的类似25kda蛋白。用免疫沉淀法对两个25kda的40s蛋白rpS5和rpS9进行特异性抗体鉴定，发现rpS5是与IRES结合的蛋白。因此，我们的研究结果支持rpS5是在翻译起始阶段将HCV RNA定位在40s核糖体亚基上的关键因素。
Translational initiation of hepatitis C virus (HCV) genome RNA occurs via its highly structured 5' noncoding region called the internal ribosome entry site (IRES), Recent studies indicate that HCV IRES and 40 S ribosomal subunit form a stable binary complex that is believed to be important for the subsequent assembly of the 48 S initiation complex. Ribosomal protein (rp) S9 has been suggested as the prime candidate protein for binding of the HCV IRES to the 40 S subunit. RpS9 has a molecular mass of similar to 25 kDa in UV cross-linking experiments. In the present study, we examined the similar to 25-kDa proteins of the 40 S ribosome that form complexes with the HCV IRES upon UV cross-linking. Immunoprecipitation with specific antibodies against two 25-kDa 40 S proteins, rpS5 and rpS9, clearly identified rpS5 as the protein bound to the IRES. Thus, our results support rpS5 as the critical element in positioning the HCV RNA on the 40 S ribosomal subunit during translation initiation.