VirA是Ti质粒指定的毒力基因的一个共调节因子，它在体外被磷酸化。
VirA, a coregulator of Ti-specified virulence genes, is phosphorylated in vitro.
作者信息
Huang Y, Morel P, Powell B, Kado C I
机构信息
Department of Plant Pathology, University of California, Davis 95616.
出版信息
J Bacteriol. 1990 Feb;172(2):1142-4. doi: 10.1128/jb.172.2.1142-1144.1990.
Abstract
High-level expression of a chimeric virA gene was obtained by replacing the first 524 codons of virA with the first half of trpE. The encoded fusion protein was isolated and found to exhibit autokinase activity. Therefore, a kinase domain is in the C-terminal portion of VirA, and protein phosphorylation may be an important feature of VirA function.
摘要
通过用色氨酸操纵子E（trpE）的前半部分替换virA的前524个密码子，获得了嵌合virA基因的高水平表达。分离出编码的融合蛋白，发现其具有自激酶活性。因此，激酶结构域位于VirA的C末端部分，蛋白质磷酸化可能是VirA功能的一个重要特征。
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