Analysis of vaccinia virus temperature-sensitive I7L mutants reveals two potential functional domains.
Analysis of vaccinia virus temperature-sensitive I7L mutants reveals two potential functional domains.
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DOI：
10.1186/1743-422x-3-64
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发表时间：
2006-08-31
期刊：
影响因子：
4.8
通讯作者：
Hruby DE
中科院分区：
文献类型：
--
作者：
Moerdyk MJ;Byrd CM;Hruby DE
作为启动牛痘病毒I7 L核心蛋白蛋白酶的结构-功能分析的方法，对其中突变已定位于I7 L位点的条件致死突变体的集合进行基因组测序和表型分析。六个牛痘病毒I7 L温度敏感突变体中的突变分为两组：在N-末端氨基酸29和37之间的三个位置处的变化和在靠近催化结构域的氨基酸344处的两个不同取代。无论突变的位置如何，在非允许温度下的突变体不能切割核心蛋白前体，并且在核心缩合之前其发育被阻止。因此，这两组突变可能影响蛋白酶活性所需的两个不同的功能结构域。
As an approach to initiating a structure-function analysis of the vaccinia virus I7L core protein proteinase, a collection of conditional-lethal mutants in which the mutation had been mapped to the I7L locus were subjected to genomic sequencing and phenotypic analyses. Mutations in six vaccinia virus I7L temperature sensitive mutants fall into two groups: changes at three positions at the N-terminal end between amino acids 29 and 37 and two different substitutions at amino acid 344, near the catalytic domain. Regardless of the position of the mutation, mutants at the non-permissive temperature failed to cleave core protein precursors and had their development arrested prior to core condensation. Thus it appears that the two clusters of mutations may affect two different functional domains required for proteinase activity.