van Heeswijk W C, Stegeman B, Hoving S, Molenaar D, Kahn D, Westerhoff H V
E.C. Slater Institute, University of Amsterdam, The Netherlands.
FEMS Microbiol Lett. 1995 Oct 1;132(1-2):153-7. doi: 10.1111/j.1574-6968.1995.tb07825.x.
The PII protein in the glutamine synthetase cascade transduces the nitrogen signal, as sensed by uridylyltransferase, both to the NRII/NRI two-component system and to adenylyltransferase, to regulate the activity of glutamine synthetase. Here we describe the amplification of a chromosomal DNA fragment from Escherichia coli which contains the sequence of a PII homologue. The derived amino acid sequence of this DNA fragment is 67% identical to E. coli PII. It contains the conserved tyrosine residue which is known to be the site of uridylylation in PII. E. coli is the first organism in which two different PII proteins have been detected.
谷氨酰胺合成酶级联反应中的PII蛋白将尿苷酰转移酶所感知的氮信号转导至NRII/NRI双组分系统和腺苷酸转移酶，以调节谷氨酰胺合成酶的活性。在此，我们描述了从大肠杆菌中扩增出一个包含PII同源物序列的染色体DNA片段。该DNA片段推导的氨基酸序列与大肠杆菌PII的同源性为67%。它含有保守的酪氨酸残基，已知该残基是PII中尿苷酰化的位点。大肠杆菌是首个检测到两种不同PII蛋白的生物体。
