Ng S C, Mertz J E, Sanden-Will S, Bina M
J Biol Chem. 1985 Jan 25;260(2):1127-32.
The predominant leader region of the late 16 S mRNAs of simian virus 40 encodes a histone-like, 61-amino acid, DNA-binding protein called the agnoprotein or LP1. To test the hypothesis that this protein facilitates assembly of viral minichromosomes into virions, we have studied the synthesis of virions in cells infected with mutants deleted in this region of the SV40 genome. We found that 220 S mature virions, indistinguishable from those of wild type, were produced in cells infected with these mutants. As in wild-type-infected cells, no assembly intermediates other than 75 S chromatin were observed. However, data obtained from both steady-state and pulse-chase labeling experiments indicated that cells infected with agnogene deletion mutants produced virions more slowly than cells infected with wild-type virus. Taken together with data showing that similar levels of virion proteins were present in the wild-type- and mutant-infected cells, these findings strongly suggest that LP1 plays a role in expediting virion assembly.
猴病毒40(SV40)晚期16S mRNA的主要前导区编码一种组蛋白样的、含61个氨基酸的DNA结合蛋白,称为agnoprotein或LP1。为了验证该蛋白促进病毒微型染色体组装进入病毒粒子这一假说,我们研究了感染了在SV40基因组该区域缺失的突变体的细胞中病毒粒子的合成。我们发现,感染这些突变体的细胞产生了与野生型无法区分的220S成熟病毒粒子。与感染野生型的细胞一样,除了75S染色质外,未观察到其他组装中间体。然而,从稳态和脉冲追踪标记实验获得的数据表明,感染agnogene缺失突变体的细胞产生病毒粒子的速度比感染野生型病毒的细胞慢。结合显示野生型和突变体感染细胞中病毒粒子蛋白水平相似的数据,这些发现有力地表明LP1在加速病毒粒子组装中起作用。