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(Received for publication, November
17, 1994; and in revised form, May 18, 1995) From the Nitrogen regulation of transcription in Escherichia coli requires sensation of the intracellular nitrogen status and
control of the dephosphorylation of the transcriptional activator
NRI
Volume 270,
Number 30,
Issue of July 28, pp. 17797-17807, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
P. This dephosphorylation is catalyzed by the bifunctional
kinase/phosphatase NRII in the presence of the dissociable PII protein.
The ability of PII to stimulate the phosphatase activity of NRII is
regulated by a signal transducing uridylyltransferase/uridylyl-removing
enzyme (UTase/UR), which converts PII to PII-UMP under conditions of
nitrogen starvation; this modification prevents PII from stimulating
the dephosphorylation of NRI
P. We used purified components to
examine the binding of small molecules to PII, the effect of small
molecules on the stimulation of the NRII phosphatase activity by PII,
the retention of PII on immobilized NRII, and the regulation of the
uridylylation of PII by the UTase/UR enzyme. Our results indicate that
PII is activated upon binding ATP and either 2-ketoglutarate or
glutamate, and that the liganded form of PII binds much better to
immobilized NRII. We also demonstrate that the concentration of
glutamine required to inhibit the uridylyltransferase activity is
independent of the concentration of 2-ketoglutarate present. We
hypothesize that nitrogen sensation in E. coli involves the
separate measurement of glutamine by the UTase/UR protein and
2-ketoglutarate by the PII protein.
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