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Abstract:

A reconstituted UTase/UR-PII-NRII-NRI bicyclic cascade regulated PII uridylylation and NRI phosphorylation in response to glutamine. We examined the sensitivity and robustness of the responses of the individual cycles and of the bicyclic system. The sensitivity of the glutamine response of the upstream UTase/UR-PII monocycle depended upon the PII concentration, and we show that PII exerted substrate inhibition of the UTase activity of UTase/UR, potentially contributing to this dependence of sensitivity on PII. In the downstream NRII-NRI monocycle, PII controlled NRI phosphorylation state, and the response to PII was hyperbolic at both saturating and unsaturating NRI concentration. As expected from theory, the level of NRI∼P produced by the NRII-NRI monocycle was robust to changes in the NRII or NRI concentrations when NRI was in excess over NRII, as long as the NRII concentration was above a threshold value, an example of absolute concentration robustness (ACR). Because of the parameters of the system, at physiological protein levels and ratios of NRI to NRII, the level of NRI∼P depended upon both protein concentrations. In bicyclic UTase/UR-PII-NRII-NRI systems, the NRI phosphorylation state response to glutamine was always hyperbolic, regardless of the PII concentration or sensitivity of the upstream UTase/UR-PII cycle. In these bicyclic systems, NRI phosphorylation state was only robust to variation in the PII/NRII ratio within a narrow range; when PII was in excess NRI∼P was low, and when NRII was in excess NRI phosphorylation was elevated, throughout the physiological range of glutamine concentrations. Our results show that the bicyclic system produced a graded response of NRI phosphorylation to glutamine under a range of conditions, and that under most conditions the response of NRI phosphorylation state to glutamine levels depended on the concentrations of NRI, NRII, and PII. © 2012 American Chemical Society.

Registro:

Documento: Artículo
Título:Characterization of the reconstituted UTase/UR-PII-NRII-NRI bicyclic signal transduction system that controls the transcription of nitrogen-regulated (Ntr) genes in Escherichia coli
Autor:Jiang, P.; Ventura, A.C.; Ninfa, A.J.
Filiación:Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606, United States
Instituto de Fisiología, Biología Molecular y Neurociencias (UBA-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2 - 2 piso, (C1428EHA) Buenos Aires, Argentina
Palabras clave:Bicyclic systems; Glutamine levels; Physiological range; Protein concentrations; Protein level; Signal transduction system; State response; Substrate inhibition; Amino acids; Escherichia coli; Phosphorylation; Physiology; Proteins; Signal transduction; Transcription; Physiological models; bacterial enzyme; glutamine; nitrogen; unclassified drug; UTase; absolute concentration robustness; article; bacterial gene; concentration (parameters); enzyme activity; Escherichia coli; genetic transcription; nonhuman; priority journal; protein modification; protein phosphorylation; signal processing; signal transduction; transcription regulation; uridylation; Bacterial Proteins; Escherichia coli; Escherichia coli Proteins; Glutamine; Multienzyme Complexes; Nitrogen; Nucleotidyltransferases; Phosphoprotein Phosphatases; PII Nitrogen Regulatory Proteins; Protein Kinases; Protein Multimerization; RNA Polymerase Sigma 54; Signal Transduction; Transcription Factors; Escherichia coli
Año:2012
Volumen:51
Número:45
Página de inicio:9045
Página de fin:9057
DOI: http://dx.doi.org/10.1021/bi300575j
Título revista:Biochemistry
Título revista abreviado:Biochemistry
ISSN:00062960
CODEN:BICHA
CAS:glutamine, 56-85-9, 6899-04-3; nitrogen, 7727-37-9; Bacterial Proteins; Escherichia coli Proteins; Glutamine, 56-85-9; Multienzyme Complexes; Nitrogen, 7727-37-9; NtrB protein, E coli; Nucleotidyltransferases, 2.7.7.-; PII Nitrogen Regulatory Proteins; PIID regulatory protein, Bacteria, 57657-57-5; Phosphoprotein Phosphatases, 3.1.3.16; Protein Kinases, 2.7.-; RNA Polymerase Sigma 54, 2.7.7.6; Transcription Factors; glnG protein, E coli; regulatory protein uridylyltransferase, 2.7.7.59; rpoN protein, E coli
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v51_n45_p9045_Jiang

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Citas:

---------- APA ----------
Jiang, P., Ventura, A.C. & Ninfa, A.J. (2012) . Characterization of the reconstituted UTase/UR-PII-NRII-NRI bicyclic signal transduction system that controls the transcription of nitrogen-regulated (Ntr) genes in Escherichia coli. Biochemistry, 51(45), 9045-9057.
http://dx.doi.org/10.1021/bi300575j
---------- CHICAGO ----------
Jiang, P., Ventura, A.C., Ninfa, A.J. "Characterization of the reconstituted UTase/UR-PII-NRII-NRI bicyclic signal transduction system that controls the transcription of nitrogen-regulated (Ntr) genes in Escherichia coli" . Biochemistry 51, no. 45 (2012) : 9045-9057.
http://dx.doi.org/10.1021/bi300575j
---------- MLA ----------
Jiang, P., Ventura, A.C., Ninfa, A.J. "Characterization of the reconstituted UTase/UR-PII-NRII-NRI bicyclic signal transduction system that controls the transcription of nitrogen-regulated (Ntr) genes in Escherichia coli" . Biochemistry, vol. 51, no. 45, 2012, pp. 9045-9057.
http://dx.doi.org/10.1021/bi300575j
---------- VANCOUVER ----------
Jiang, P., Ventura, A.C., Ninfa, A.J. Characterization of the reconstituted UTase/UR-PII-NRII-NRI bicyclic signal transduction system that controls the transcription of nitrogen-regulated (Ntr) genes in Escherichia coli. Biochemistry. 2012;51(45):9045-9057.
http://dx.doi.org/10.1021/bi300575j