脑心肌炎病毒多聚蛋白编码区的核苷酸序列及推导的氨基酸序列。
The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region.
作者信息
Palmenberg A C, Kirby E M, Janda M R, Drake N L, Duke G M, Potratz K F, Collett M S
出版信息
Nucleic Acids Res. 1984 Mar 26;12(6):2969-85. doi: 10.1093/nar/12.6.2969.
Abstract
The nucleotide sequence of 7200 bases of encephalomyocarditis (EMC) viral RNA, including the complete polyprotein-coding region, was determined. The polyprotein is encoded within a unique translational reading frame, 6870 bases in length. Protein synthesis begins with the sequence Met-Ala-Thr, and ends with the sequence Leu-Phe-Trp, 126 bases from the 3' end of the RNA. Viral capsid and noncapsid proteins were aligned with the deduced amino acid sequence of the polyprotein. The proteolytic processing map follows the standard 4-3-4 picornaviral pattern except for a short leader peptide (8 kd), which precedes the capsid proteins. Identification of the proteolytic cleavage sites showed that EMC viral protease, p22, has cleavage specificity for gln-gly or gln-ser sequences with adjacent proline residues. The cleavage specificity of the host-coded protease(s) includes both tyr-pro and gln-gly sequences.
摘要
测定了脑心肌炎（EMC）病毒RNA 7200个碱基的核苷酸序列，包括完整的多聚蛋白编码区。多聚蛋白由一个独特的翻译阅读框编码，长度为6870个碱基。蛋白质合成起始于序列Met-Ala-Thr，终止于RNA 3'端126个碱基处的序列Leu-Phe-Trp。病毒衣壳蛋白和非衣壳蛋白与推导的多聚蛋白氨基酸序列进行了比对。除了在衣壳蛋白之前有一个短的前导肽（8kd）外，蛋白水解加工图谱遵循标准的4-3-4微小核糖核酸病毒模式。对蛋白水解切割位点的鉴定表明，EMC病毒蛋白酶p22对具有相邻脯氨酸残基的gln-gly或gln-ser序列具有切割特异性。宿主编码蛋白酶的切割特异性包括tyr-pro和gln-gly序列。
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