An additional PII in Escherichia coli: a new regulatory protein in the glutamine synthetase cascade |
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| Authors: | Wally C van Heeswijk Brenda Stegeman Sjouke Hoving Douwe Molenaar Daniel Kahn Hans V Westerhoff |
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| Institution: | E. C. Slater Institute, University of Amsterdam, Plantage Muidergracht 12, NL-1018 TV Amsterdam, The Netherlands; Division of Molecular Biology (H5), The Netherlands Cancer Institute, Plesmanlaan 121, NL-1066 CX Amsterdam, The Netherlands; Laboratoire de Biologie Moléculaire des Relations-Plantes Microorganismes, CNRS-INRA, BP27, 31326 Castanet-Tolosan Cedex, France |
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| Abstract: | Abstract 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. |
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| Keywords: | PII-protein Glnb Glutamine synthetase Signal transduction Ammonia assimilation Nitrogen regulation Escherichia coli |
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