Shiau S P, Schneider B L, Gu W, Reitzer L J
Program in Molecular and Cell Biology, University of Texas at Dallas, Richardson 75083-0688.
J Bacteriol. 1992 Jan;174(1):179-85. doi: 10.1128/jb.174.1.179-185.1992.
During nitrogen-limited growth, transcription of glnA, which codes for glutamine synthetase, requires sigma 54-RNA polymerase and the phosphorylated from the nitrogen regulator I (NRI; also called NtrC). In cells in which the lac promoter controlled expression of the gene coding for NRI, increasing the intracellular concentration of NRI lowered the level of glutamine synthetase. The reduction in glutamine synthetase does not appear to result from the NRI-dependent sequestering of any protein that affects transcription of glnA. Our results also suggest that the negative effect of a high concentration of NRI on glnA expression is a major determinant of the level of glutamine synthetase activity in nitrogen-limited cells of a wild-type strain. We propose that the inhibition results from an impairment of the interaction between NRI-phosphate and RNA polymerase that stimulates glnA transcription. We discuss a model that can account for this reduction in glutamine synthetase.
在氮限制生长期间,编码谷氨酰胺合成酶的glnA的转录需要σ54-RNA聚合酶以及来自氮调节因子I(NRI;也称为NtrC)的磷酸化形式。在lac启动子控制NRI编码基因表达的细胞中,增加细胞内NRI的浓度会降低谷氨酰胺合成酶的水平。谷氨酰胺合成酶的减少似乎不是由于NRI依赖的对任何影响glnA转录的蛋白质的隔离。我们的结果还表明,高浓度NRI对glnA表达的负面影响是野生型菌株氮限制细胞中谷氨酰胺合成酶活性水平的主要决定因素。我们提出这种抑制是由于刺激glnA转录的NRI-磷酸与RNA聚合酶之间的相互作用受损所致。我们讨论了一个可以解释谷氨酰胺合成酶这种减少的模型。