Nellemann L J, Holm F, Atlung T, Hansen F G
Department of Microbiology, Technical University of Denmark, Lyngby.
Gene. 1989 Apr 15;77(1):185-91. doi: 10.1016/0378-1119(89)90373-9.
The pgk gene of Escherichia coli coding for the phosphoglycerate kinase was subcloned from the Carbon and Clarke collection plasmid pLC33-5. The position and direction of transcription of the pgk gene was determined by Tn5 insertion mutagenesis. Analysis of proteins encoded from these plasmids showed that the pgk gene product is a 40-kDa protein, and that the gene is transcribed from two promoters, one immediately in front of the gene and one in front of an upstream gene coding for a 38-kDa polypeptide of unknown function. The position of the Pgk protein on two-dimensional O'Farrel gels was identified, and from this we conclude that it is one of the proteins induced by anaerobiosis [Smith and Neidhardt, J. Bacteriol. 154 (1987) 336-343]. The pgk gene was also found to show growth phase regulation; the synthesis of Pgk protein was induced more than ten-fold during transition from the exponential to the stationary growth phase.
编码磷酸甘油酸激酶的大肠杆菌pgk基因是从卡尔本和克拉克文库的质粒pLC33 - 5中克隆出来的。通过Tn5插入诱变确定了pgk基因的转录位置和方向。对这些质粒所编码蛋白质的分析表明，pgk基因产物是一种40 kDa的蛋白质，并且该基因由两个启动子转录，一个紧邻该基因前方，另一个位于上游一个编码功能未知的38 kDa多肽的基因前方。确定了Pgk蛋白在二维奥法雷尔凝胶上的位置，据此我们得出结论，它是一种由厌氧诱导产生的蛋白质[史密斯和尼德哈特，《细菌学杂志》154(1987)336 - 343]。还发现pgk基因呈现生长阶段调控；在从指数生长期向稳定期转变期间，Pgk蛋白的合成被诱导了十多倍。
