Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in Escherichia coli.

Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in Escherichia coli.
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CRP训练营和PII-NTR系统之间的相互作用形成了大肠杆菌中碳代谢和氮同化之间的新调节网络。

DOI:
10.1093/nar/gkl1142
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发表时间:
2007
影响因子:
14.9
通讯作者:
Wang, Yi-Ping
Wang, Yi-Ping
中科院分区:
生物学2区
文献类型:
--
作者:
Mao, Xian-Jun;Huo, Yi-Xin;Buck, Martin;Kolb, Annie;Wang, Yi-Ping

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在大肠杆菌中,碳源的利用受到磷酸烯醇丙酮酸依赖性磷酸转移酶系统 (PTS) 的调节,该系统调节细胞内 cAMP 的水平。 cAMP 受体蛋白 (CRP) 控制许多分解代谢基因的转录。 PII 蛋白在细胞内谷氨酰胺水平上感知氮的可用性。谷氨酰胺主要由GlnHPQ转运,并由glnA编码的谷氨酰胺合成酶(GS)合成。先前的研究表明,CRP 会影响氮同化。在这里,我们表明至少涉及两种机制。首先,CRP 通过与 sigma 70 RNA 聚合酶 (Eσ70) 协同结合激活 glnHp1 并抑制 glnHp2。因此,在存在谷氨酰胺的情况下,glnHPQ 表达的整体增强会改变 GlnB 信号传导并使 glnAp2 失活。其次,体外研究表明,CRP 可以被 sigma 54 全酶 (Eσ54) 招募到以 glnAp2 上游 -51.5 为中心的位点。 CRP 诱导的 DNA 弯曲可防止氮调节蛋白 C (NtrC) 激活剂接近启动子结合的 Eσ54 闭合复合物的激活剂可及面,并抑制 glnAp2。因此,作为“葡萄糖效应”的主要转录效应子,CRP既影响信号转导途径,又影响氮调节子转录机制的整体几何结构。
In Escherichia coli, utilization of carbon sources is regulated by the phosphoenolpyruvate-dependent phosphotransferase system (PTS), which modulates the intracellular levels of cAMP. The cAMP receptor protein (CRP) controls the transcription of many catabolic genes. The availability of nitrogen is sensed by the PII protein at the level of intracellular glutamine. Glutamine is transported mainly by GlnHPQ, and synthesized by glutamine synthetase (GS) encoded by glnA. Previous studies suggest that CRP affects nitrogen assimilation. Here we showed that at least two mechanisms are involved. First, CRP activates glnHp1 via synergistic binding with sigma 70 RNA polymerase (Eσ70) and represses glnHp2. As a consequence, in the presence of glutamine, the overall enhancement of glnHPQ expression alters GlnB signalling and de-activates glnAp2. Second, in vitro studies show that CRP can be recruited by sigma 54 holoenzyme (Eσ54) to a site centred at −51.5 upstream of glnAp2. CRP-induced DNA-bending prevents the nitrogen regulation protein C (NtrC) activator from approaching the activator-accessible face of the promoter-bound Eσ54 closed complex, and inhibits glnAp2. Therefore, as the major transcriptional effector of the ‘glucose effect’, CRP affects both the signal transduction pathway and the overall geometry of the transcriptional machinery of components of the nitrogen regulon.
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