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.

Keener, John; Kustu, Sydney

doi:10.1073/pnas.85.14.4976

Cited by 345 publications

(318 citation statements)

References 18 publications

(17 reference statements)

Supporting

Mentioning

307

Contrasting

Unclassified

Order By: Relevance

“…The HK then binds and transfers its phosphoryl group to a response regulator (RR), which often functions directly as a transcription factor, regulating gene expression patterns in response to the signal (1,2). Many HKs are bifunctional, acting as both the kinase and phosphatase for their RR; the ratio of kinase to phosphatase activity, and thus the phosphorylation state of the RR, is controlled by the input (1)(2)(3)(4)(5)(6)(7)(8).…”

mentioning

confidence: 99%

Crosstalk and the evolution of specificity in two-component signaling

Rowland

Deeds

2014

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Significance The global architectures of signaling networks in bacteria and eukaryotes are remarkably different: crosstalk between pathways is very common in eukaryotes but is very limited in bacteria. Bacteria use two-component signaling (TCS) to transduce information, relying on a single enzyme to act as both kinase and phosphatase for targets. We used mathematical models to show that introducing crosstalk in TCS always decreases system performance. This indicates that the large-scale differences between eukaryotic and bacterial networks likely derive from differences in the dynamics of the fundamental motifs from which the networks themselves are constructed. We further demonstrated that the pressure to avoid crosstalk has influenced the evolution of new TCS pairs, driving rapid sequence divergence in protein interaction interfaces immediately postduplication.

show abstract

mentioning

confidence: 99%

Crosstalk and the evolution of specificity in two-component signaling

Rowland

Deeds

2014

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…NR, phosphorylation is catalyzed by NR,, which also has NR,,-phosphatase activity [39-411. This activity is stimulated by a protein, P,, [40]. P,, is subject to modification by uridylylation on a tyrosine residue [42].…”

Section: Cascade Controlmentioning

confidence: 99%

Energy, control and DNA structure in the living cell

Wijker

Jensen

Snoep

et al. 1995

Biophysical Chemistry

View full text Add to dashboard Cite

Energy, control and DNA structure in the living cell. General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. ratio is essential to overcome the thermodynamic burden 01 uphill processes, it is not clear to what degree enzymes that control this ratio also control cell physiology. Indeed. in the living cell homeostatic control mechanisms might exist for the free-energy transduction pathways so as to prevent perturbation of cellular function when the Gibbs energy supply is compromised. This presentation addresses the extent to which the intracellular ATP level is involved in the control of cell physiology, how the elaborate control of cell function may be analyzed theoretically and quantitatively, and if this can be utilized selectively to affect certain cell types.

show abstract

“…Rapid hydrolysis in vitro is the hallmark of an acyl phosphate; prothymosin ␣ loses its glutamyl phosphates, which were acquired in vivo, almost instantaneously upon cell lysis, and the aspartyl phosphates of Che Y (39) and NtrC (40,41), which were labeled in vitro under carefully defined conditions, disappear with halflives of ϳ6 s and 3.5 min, respectively. Che Y and NtrC, each with one aspartyl phosphate, are examples of bacterial response regulator proteins, which comprise the second member of two-component systems (reviewed in Refs.…”

mentioning

confidence: 99%

Prothymosin α in Vivo Contains Phosphorylated Glutamic Acid Residues

Trumbore

Wang

Enkemann

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

2) Immediately upon cell lysis, the pH stability curves of metabolically labeled native [ 32 P]prothymosin ␣ or a [ 32 P]histidine-tagged variant resembled the pH stability curve of acetyl phosphate. 3) After a brief incubation at pH 7, these curves changed from a pattern diagnostic for an acyl phosphate to that characteristic of a serine or threonine phosphate, an observation consistent with transfer of phosphate in vitro. Our data indicate that most of prothymosin ␣'s phosphates are subject instantaneously to hydrolysis, based on the observation that greater than 90% of the phosphate initially found at pH 7 disappeared at the extremes of pH. Rapid loss of phosphate was not affected by the presence of phosphatase inhibitors including 50 mM sodium fluoride, 1 mM okadaic acid, and 0.5 mM calyculin A. The amount of phosphate missing could not be ascertained, but the trifling amount recovered on Ser or Thr depended heavily on conditions favoring the transient survival of labile phosphate. Further analysis using COS cells lysed in the presence of sodium borohydride showed that: 1) phosphate recovered on prothymosin ␣ decreased 8-fold when lysates were treated with borohydride; 2) the reagent caused 4 -8 glutamic acid residues/molecule to vanish; 3) using [ 3 H]NaBH 4 , label was introduced into proline, a product derived from reductive cleavage of phosphoglutamate; and 4) [ 3 H]proline was localized almost exclusively to a peptide with pronounced homology to the histone binding site of nucleoplasmin, a chromatin remodeling protein found in Xenopus laevis. Our data demonstrate that prothymosin ␣ is energy-rich by virtue of stoichiometric amounts of glutamyl phosphate.Prothymosin ␣ is a highly unusual protein with an unfortunate name. The protein is neither a precursor for processed polypeptides nor specifically associated with the thymus nor a member of a family with ␤ or ␥ homologues (1-3). Instead, it is probably the most acidic naturally occurring polypeptide in the eukaryotic world, with 54 carboxyl groups in 109 amino acids, resulting in an isoelectric point at or below pH 3.5 (1, 2, 4). The mRNA for prothymosin ␣ is distributed ubiquitously among mammalian nucleated cells and tissues (1). The protein possesses a potent nuclear localization signal and is present in amounts equivalent to those of histone H1 (5, 6). Because the amount of prothymosin ␣ mRNA (and presumably protein) found in a cell is directly proportional to cell growth, the protein is believed to play a role in cell proliferation (1). This idea was reinforced by the observation that synchronized human myeloma cells, in the presence of antisense oligodeoxyribonucleotides directed at prothymosin ␣ mRNA, were unable to divide while detectable amounts of the antisense oligonucleotides remained inside the cell (7). There are now many examples of a link between prothymosin ␣ and growth in systems as diverse as developing mouse embryos (8); normal, mitogenstimulated, and malignant lymphocytes (9, 10); and regenerating liver (10). There are also positive ...

show abstract

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.

Cited by 345 publications

References 18 publications

Crosstalk and the evolution of specificity in two-component signaling

Crosstalk and the evolution of specificity in two-component signaling

Energy, control and DNA structure in the living cell

Prothymosin α in Vivo Contains Phosphorylated Glutamic Acid Residues

Contact Info

Product

Resources

About