Gebhardt K, King R A, Christie G E, Lindqvist B H
Institute of Biology, University of Oslo, Norway.
J Bacteriol. 1993 Dec;175(23):7724-6. doi: 10.1128/jb.175.23.7724-7726.1993.
The Ogr protein is a 72-residue, zinc-binding transcription factor essential for activation of late gene expression in bacteriophage P2. Analysis of C-terminal truncated proteins generated by stop codon mutagenesis shows that deletion of residues distal to position 51 had negligible effects on Ogr function. More-extensive deletion resulted in unstable products with severely reduced activity. These results, as well as the effects of other mutations in this region, support the idea that the 21 C-terminal residues are not required for transactivation.
Ogr蛋白是一种由72个氨基酸残基组成的锌结合转录因子，对噬菌体P2晚期基因表达的激活至关重要。通过终止密码子诱变产生的C末端截短蛋白分析表明，删除51位远端的残基对Ogr功能的影响可忽略不计。更广泛的删除导致产物不稳定，活性严重降低。这些结果以及该区域其他突变的影响支持了这样一种观点，即反式激活不需要21个C末端残基。
