scholarly journals Cyclic AMP Receptor Protein and TyrR Are Required for Acid pH and Anaerobic Induction of hyaB andaniC in Salmonella typhimurium

1999 ◽  
Vol 181 (2) ◽  
pp. 689-694 ◽  
Author(s):  
Kyeong R. Park ◽  
Jean-Christophe Giard ◽  
Juno H. Eom ◽  
Shawn Bearson ◽  
John W. Foster
Keyword(s):  
Amino Acid ◽  
Cyclic Amp ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Positive Regulators ◽  
Aromatic Amino Acid Metabolism ◽  
Camp Receptor ◽  
Inducible Genes

ABSTRACT Two acid-inducible genes, aniC and aciK, that require anaerobiosis and tyrosine for expression were identified as orf326a encoding a potential amino acid/polyamine antiporter and hyaB encoding hydrogenase I, respectively. Cyclic AMP (cAMP) receptor protein, cAMP, and TyrR, regulator of aromatic amino acid metabolism, were strong positive regulators of both genes.

scholarly journals Cyclic AMP Directly Activates NasP, an N-Acyl Amino Acid Antibiotic Biosynthetic Enzyme Cloned from an Uncultured β-Proteobacterium

2007 ◽  
Vol 189 (17) ◽  
pp. 6487-6489 ◽  
Author(s):  
Jon Clardy ◽  
Sean F. Brady
Keyword(s):  
Amino Acid ◽  
Cyclic Amp ◽  
Gene Sequence ◽  
Protein A ◽  
Environmental Dna ◽  
Receptor Protein ◽  
Rrna Gene ◽  
Camp Receptor Protein ◽  
Nucleotide Binding Domain ◽  
Camp Receptor

ABSTRACT The cyclic AMP (cAMP)-dependent biosynthesis of N-acylphenylalanine antibiotics by NasP, an environmental DNA-derived N-acyl amino acid synthase, is controlled by an NasP-associated cyclic nucleotide-binding domain and is independent of the global cAMP signal transducer, cAMP receptor protein. A 16S rRNA gene sequence found on the same environmental DNA cosmid as NasP is most closely related to 16S sequences from β-proteobacteria.

Aromatic amino acid metabolism of neonatal piglets receiving TPN: effect of tyrosine precursors

1994 ◽  
Vol 267 (5) ◽  
pp. E672-E679 ◽  
Author(s):  
L. J. Wykes ◽  
J. D. House ◽  
R. O. Ball ◽  
P. B. Pencharz
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Central Line ◽  
High Plasma ◽  
Control Group ◽  
Neonatal Piglets ◽  
Aromatic Amino Acid Metabolism ◽  
Plasma Tyrosine

Low tyrosine solubility in total parenteral nutrition (TPN) solutions complicates meeting the aromatic amino acid needs of infants. This study compared the effectiveness of two tyrosine precursors to supply the aromatic amino acid needs of TPN-fed neonatal piglets with a control group in which total aromatic acid needs were met by the addition of phenylalanine (Phe). Eighteen 3-day-old male Yorkshire piglets (6/group) received TPN for 8 days by central line. The solution was supplemented with Phe or one of the following two tyrosine precursors: N-acetyltyrosine (N-AcTyr) or glycyltyrosine (GlyTyr). Aromatic amino acid metabolism, growth, and nitrogen utilization were measured. Average amino acid and energy intakes were 14.6 g.kg-1.day-1 and 1,050 kJ.kg-1.day-1. Nitrogen balance and utilization were significantly higher (P < 0.05) in piglets in the control Phe group and on the GlyTyr regimen. The high urinary excretion of N-AcTyr (65%) confirms its low bioavailability. Flux and oxidation were significantly higher (P < 0.05) in the Phe group. High plasma Phe levels and excretion of Phe catabolites, as well as the high plasma tyrosine in the GlyTyr group, indicate that current strategies employed to meet the aromatic amino acid needs of neonates on TPN need further refinement.

scholarly journals The cyclic AMP (cAMP)-cAMP receptor protein complex functions both as an activator and as a corepressor at the tsx-p2 promoter of Escherichia coli K-12.

1991 ◽  
Vol 173 (17) ◽  
pp. 5419-5430 ◽  
Author(s):  
P Gerlach ◽  
L Søgaard-Andersen ◽  
H Pedersen ◽  
J Martinussen ◽  
P Valentin-Hansen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cyclic Amp ◽  
Protein Complex ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Complex Functions ◽  
P2 Promoter ◽  
Camp Receptor ◽  
K 12

scholarly journals Deletion of a Cyclic AMP Receptor Protein Homologue Diminishes Germination and Affects Morphological Development of Streptomyces coelicolor

2004 ◽  
Vol 186 (6) ◽  
pp. 1893-1897 ◽  
Author(s):  
A. Derouaux ◽  
S. Halici ◽  
H. Nothaft ◽  
T. Neutelings ◽  
G. Moutzourelis ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Streptomyces Coelicolor ◽  
Regulatory Proteins ◽  
Receptor Protein ◽  
Growth Delay ◽  
Morphological Development ◽  
Camp Receptor Protein ◽  
Reading Frame ◽  
Physiological Processes ◽  
Camp Receptor

ABSTRACT Open reading frame SCO3571 of Streptomyces coelicolor encodes a protein of the cyclic AMP (cAMP) receptor protein (CRP) superfamily of regulatory proteins. A mutant revealed a dramatic defect in germination, followed by growth delay and earlier sporulation. This phenotype correlates with those of an adenylate cyclase (cya) mutant that cannot synthesize cAMP. This finding suggests that S. coelicolor may use a Cya-cAMP-CRP system to trigger complex physiological processes such as morphogenesis.

scholarly journals Suppression of Virulence of Toxigenic Vibrio cholerae by Anethole through the Cyclic AMP (cAMP)-cAMP Receptor Protein Signaling System

PLoS ONE ◽  
2015 ◽  
Vol 10 (9) ◽  
pp. e0137529 ◽  
Author(s):  
M. Shamim Hasan Zahid ◽  
Sharda Prasad Awasthi ◽  
Masahiro Asakura ◽  
Shruti Chatterjee ◽  
Atsushi Hinenoya ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Vibrio Cholerae ◽  
Receptor Protein ◽  
Protein Signaling ◽  
Camp Receptor Protein ◽  
Signaling System ◽  
Camp Receptor

scholarly journals Regulation of ytfK by cAMP-CRP Contributes to SpoT-Dependent Accumulation of (p)ppGpp in Response to Carbon Starvation YtfK Responds to Glucose Exhaustion

2021 ◽  
Vol 12 ◽  
Author(s):  
Laura Meyer ◽  
Elsa Germain ◽  
Etienne Maisonneuve
Keyword(s):  
Escherichia Coli ◽  
Cyclic Amp ◽  
Catabolite Repression ◽  
Stringent Response ◽  
Receptor Protein ◽  
Glucose Starvation ◽  
Camp Receptor Protein ◽  
E Coli ◽  
Camp Receptor ◽  
Glucose Availability

Guanosine penta- or tetraphosphate (known as (p)ppGpp) serves as second messenger to respond to nutrient downshift and other environmental stresses, a phenomenon called stringent response. Accumulation of (p)ppGpp promotes the coordinated inhibition of macromolecule synthesis, as well as the activation of stress response pathways to cope and adapt to harmful conditions. In Escherichia coli, the (p)ppGpp level is tightly regulated by two enzymes, the (p)ppGpp synthetase RelA and the bifunctional synthetase/hydrolase SpoT. We recently identified the small protein YtfK as a key regulator of SpoT-mediated activation of stringent response in E. coli. Here, we further characterized the regulation of ytfK. We observed that ytfK is subjected to catabolite repression and is positively regulated by the cyclic AMP (cAMP)-cAMP receptor protein (CRP) complex. Importantly, YtfK contributes to SpoT-dependent accumulation of (p)ppGpp and cell survival in response to glucose starvation. Therefore, regulation of ytfK by the cAMP-CRP appears important to adjust (p)ppGpp level and coordinate cellular metabolism in response to glucose availability.

scholarly journals Halogenated tryptophan derivatives disrupt essential transamination mechanisms in bloodstream form Trypanosoma brucei

2020 ◽  
Vol 14 (12) ◽  
pp. e0008928
Author(s):  
Peter E. Cockram ◽  
Emily A. Dickie ◽  
Michael P. Barrett ◽  
Terry K. Smith
Keyword(s):  
Amino Acid ◽  
Trypanosoma Brucei ◽  
Amino Acid Metabolism ◽  
Human African Trypanosomiasis ◽  
Acid Metabolism ◽  
Aromatic Amino Acids ◽  
Parasite Survival ◽  
Aromatic Amino Acid Metabolism ◽  
Tryptophan Analogues ◽  
Tryptophan Derivatives

Amino acid metabolism within Trypanosoma brucei, the causative agent of human African trypanosomiasis, is critical for parasite survival and virulence. Of these metabolic processes, the transamination of aromatic amino acids is one of the most important. In this study, a series of halogenated tryptophan analogues were investigated for their anti-parasitic potency. Several of these analogues showed significant trypanocidal activity. Metabolomics analysis of compound-treated parasites revealed key differences occurring within aromatic amino acid metabolism, particularly within the widely reported and essential transamination processes of this parasite.

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