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Protein Kinase and Phosphoprotein Phosphatase Activities of Nitrogen Regulatory Proteins NTRB and NTRC of Enteric Bacteria: Roles of the Conserved Amino-Terminal Domain of NTRC

J. Keener and S. Kustu
Proceedings of the National Academy of Sciences of the United States of America
Vol. 85, No. 14 (Jul. 15, 1988), pp. 4976-4980
Stable URL: http://www.jstor.org/stable/32341
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Protein Kinase and Phosphoprotein Phosphatase Activities of Nitrogen Regulatory Proteins NTRB and NTRC of Enteric Bacteria: Roles of the Conserved Amino-Terminal Domain of NTRC
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Abstract

The NTRC protein (ntrC product) of enteric bacteria activates transcription of nitrogen-regulated genes by a holoenzyme form of RNA polymerase that contains the ntrA product (σ 54) as σ factor. Although unmodified NTRC will bind to DNA, it must be phosphorylated to activate transcription. Both phosphorylation and dephosphorylation of NTRC occur in the presence of the NTRB protein (ntrB product). We here demonstrate rigorously that it is the NTRB protein that is a protein kinase by showing that NTRB can phosphorylate itself, whereas NTRC cannot. Phosphorylated NTRC (NTRC-P) is capable of autodephosphorylation with a first-order rate constant of 0.14-0.19 min-1 (t1/2 of 5.0-3.6 min) at 37 degrees C. In addition, there is regulated dephosphorylation of NTRC-P. By contrast to the autophosphatase activity, regulated dephosphorylation requires three components in addition to NTRC-P: the PII regulatory protein, NTRB, and ATP. NTRC is phosphorylated within its amino-terminal domain, which is conserved in one partner of a number of two-component regulatory systems in a wide variety of eubacteria. A purified aminoterminal fragment of NTRC (≈ 12.5 kDa) is sufficient for recognition by NTRB and is autodephosphorylated at the same rate as the native protein.

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