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首页> 外文期刊>Biochemistry >Escherichia coli PII Signal Transduction Protein Controlling Nitrogen Assimilation Acts As a Sensor of Adenylate Energy Charge in Vitro
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Escherichia coli PII Signal Transduction Protein Controlling Nitrogen Assimilation Acts As a Sensor of Adenylate Energy Charge in Vitro

机译：大肠杆菌PII信号转导蛋白控制氮同化充当体外腺苷酸能量电荷的传感器。

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摘要

PII signal transduction proteins are among the most widely distributed signaling proteins in nature,controlling nitrogen assimilation in organisms ranging from bacteria to higher plants.PII proteins integrate signals of cellular metabolic status and interact with and regulate receptors that are signal transduction enzymes or key metabolic enzymes.Prior work with Escherichia coli PII showed that all signal transduction functions of PII required ATP binding to PII and that ATP binding was synergistic with the binding of alpha-ketoglutarate to PII.Furthermore,alpha-ketoglutarate,a cellular signal of nitrogen and carbon status,was observed to strongly regulate PII functions.Here,we show that in reconstituted signal transduction systems,ADP had a dramatic effect on PII regulation of two E.coli PII receptors,ATase,and NPII(NtrB),and on PII uridylylation by the signal transducing UTase/UR.ADP acted antagonistically to alpha-ketoglutarate,that is,low adenylylate energy charge acted to diminish signaling of nitrogen limitation.By individually studying the interactions that occur in the reconstituted signal transduction systems,we observed that essentially all PII and PII-UMP interactions were influenced by ADP.Our experiments also suggest that under certain conditions,the three nucleotide binding sites of the PII trimer may be occupied by combinations of ATP and ADP.In the aggregate,our results show that PII proteins,in addition to serving as sensors of alpha-ketoglutarate,have the capacity to serve as direct sensors of the adenylylate energy charge.
机译：PII信号转导蛋白是自然界中分布最广泛的信号蛋白之一，可控制从细菌到高等植物等生物体中的氮同化。PII蛋白整合细胞代谢状态信号，并与信号转导酶或关键代谢酶受体相互作用并对其进行调节。与大肠杆菌PII的先验工作表明，PII的所有信号转导功能都需要ATP与PII结合，并且ATP结合与α-酮戊二酸与PII的结合具有协同作用。我们观察到，ADP在重构的信号转导系统中，对两种大肠杆菌PII受体ATase和NPII（NtrB）的PII调节以及对PII尿苷酸化有显着影响。信号转导UTase / UR.ADP对α-酮戊二酸起拮抗作用，即低腺苷酸能电荷起减少作用通过单独研究重构信号转导系统中发生的相互作用，我们观察到基本上所有PII和PII-UMP相互作用均受ADP的影响。我们的实验还表明，在一定条件下，氮的三个核苷酸结合位点总的来说，我们的结果表明，PII蛋白除了可以作为α-酮戊二酸的传感器外，还可以作为腺苷酸能量电荷的直接传感器。

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