Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon.
Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon.
复制标题
甲病毒非结构蛋白的序列编码被蛋白石终止密码子中断。
DOI：
10.1073/pnas.80.17.5271
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发表时间：
1983
影响因子：
11.1
通讯作者：
Strauss,JH
中科院分区：
文献类型：
--
作者：
Strauss,EG;Rice,CM;Strauss,JH
我们已经获得了两种甲病毒，辛德毕斯病毒和米德尔堡病毒，在一个广泛的区域编码的非结构（复制酶）蛋白的基因组RNA的核苷酸序列。在这两种病毒中，在相同的位置，蛋白石（UGA）终止密码子打断了一个长的开放阅读框架。非结构蛋白被翻译为多蛋白前体，其通过翻译后切割加工成四条多肽链;这里提供的序列数据表明，COOH末端多肽ns 72可以通过通读该蛋白石密码子产生。这两种病毒的ns 72多肽之间的高度氨基酸同源性，相反，缺乏保守的序列上游的通读网站，表明ns 72在病毒复制中起着重要的作用，可能调节其他复制酶成分的行动。
We have obtained the nucleotide sequence of the genomic RNAs of two alphaviruses, Sindbis virus and Middelburg virus, over an extensive region encoding the nonstructural (replicase) proteins. In both viruses in an equivalent position an opal (UGA) termination codon punctuates a long otherwise open reading frame. The nonstructural proteins are translated as polyprotein precursors that are processed by posttranslational cleavage into four polypeptide chains; the sequence data presented here indicate that the COOH-terminal polypeptide, ns72, may be produced by read-through of this opal codon. The high degree of amino acid homology between the ns72 polypeptides of the two viruses, in contrast to the lack of conserved sequence upstream from the read-through site, suggests that ns72 plays an important role in viral replication, possibly modulating the action of other replicase components.