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Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism.

机译:细菌趋化性信号转导蛋白与Ntr调节子的转录调节剂之间的串扰:证据表明氮的同化和趋化性是由常见的磷转移机制控制的。

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摘要

We demonstrate by using purified bacterial components that the protein kinases that regulate chemotaxis and transcription of nitrogen-regulated genes, CheA and NRII, respectively, have cross-specificities: CheA can phosphorylate the Ntr transcription factor NRI and thereby activate transcription from the nitrogen-regulated glnA promoter, and NRII can phosphorylate CheY. In addition, we find that a high intracellular concentration of a highly active mutant form of NRII can suppress the smooth-swimming phenotype of a cheA mutant. These results argue strongly that sensory transduction in the Ntr and Che systems involves a common protein phosphotransfer mechanism.
机译:我们通过使用纯化的细菌成分证明,分别调节趋化性和氮调控基因CheA和NRII转录的蛋白激酶具有交叉特异性:CheA可以磷酸化Ntr转录因子NRI,从而激活氮调控的转录glnA启动子和NRII可以磷酸化CheY。此外,我们发现高细胞内浓度的高活性突变体形式的NRII可以抑制cheA突变体的平稳游泳表型。这些结果强烈表明,Ntr和Che系统中的感官转导涉及一种常见的蛋白质磷酸转移机制。

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