MacFarlane S A, Merrick M J
AFRC Unit of Nitrogen Fixation, University of Sussex, Brighton, UK.
Mol Microbiol. 1987 Sep;1(2):133-42. doi: 10.1111/j.1365-2958.1987.tb00505.x.
A number of in-frame insertion and deletion mutations have been constructed in vitro in the Klebsiella pneumoniae ntrB gene and the effects of each mutant NtrB protein on NtrC activity have been assessed after reintroduction of the ntrB mutation into the glnA ntrBC operon. These experiments suggest that the phosphorylation of NtrC catalysed by NtrB not only makes NtrC competent as a transcriptional activator but also improves the DNA-binding properties and hence the negative control functions of NtrC. The variety of NtrB phenotypes obtained suggest a structure/function model for the protein.
已在体外构建了肺炎克雷伯菌ntrB基因的一些框内插入和缺失突变,并将ntrB突变重新引入glnA ntrBC操纵子后,评估了每个突变型NtrB蛋白对NtrC活性的影响。这些实验表明,由NtrB催化的NtrC磷酸化不仅使NtrC具备作为转录激活因子的能力,还改善了DNA结合特性,从而增强了NtrC的负调控功能。获得的多种NtrB表型提示了该蛋白的结构/功能模型。