Hunt D M, Emerson S U, Wagner R R
J Virol. 1976 May;18(2):596-603. doi: 10.1128/JVI.18.2.596-603.1976.
In vitro transcriptase activity of three group I temperature-sensitive (ts) mutants of vesicular stomatitis virus restricted at 39 C was restored by L-protein fractions derived from wild-type (wt) vesicular stomatitis virion nucleo-capsids. Soluble NS protein from wt nucleocapsids did not reconstitute restricted transcriptions of the group I RNA-ts mutants. NS protein activity, but not L protein activity, was purified from the group I ts mutants; this NS fraction always displayed the wt phenotype in reconstitution assays. Neither the L nor the NS protein was capable of restoring the defective transcriptive activity of the group IV vesicular stomatitis virus mutant ts W16B.
在39℃受到限制的水泡性口炎病毒的三个I组温度敏感(ts)突变体的体外转录酶活性,可通过源自野生型(wt)水泡性口炎病毒粒子核衣壳的L蛋白组分恢复。来自wt核衣壳的可溶性NS蛋白不能重建I组RNA-ts突变体的受限转录。从I组ts突变体中纯化出了NS蛋白活性而非L蛋白活性;该NS组分在重组试验中始终表现出wt表型。L蛋白和NS蛋白均不能恢复IV组水泡性口炎病毒突变体ts W16B的缺陷转录活性。