scholarly journals cAMP receptor protein (CRP) positively regulates the yihU–yshA operon in Salmonella enterica serovar Typhi

Microbiology ◽  
2011 ◽  
Vol 157 (3) ◽  
pp. 636-647 ◽  
Author(s):  
J. M. Villarreal ◽  
I. Hernández-Lucas ◽  
F. Gil ◽  
I. L. Calderón ◽  
E. Calva ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Salmonella Enterica ◽  
Regulatory Region ◽  
Enteric Bacteria ◽  
Transcriptional Unit ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Salmonella Enterica Serovar Typhi ◽  
Genetic Components ◽  
Camp Receptor

Salmonella enterica serovar Typhi (S. Typhi) is the aetiological agent of typhoid fever in humans. This bacterium is also able to persist in its host, causing a chronic disease by colonizing the spleen, liver and gallbladder, in the last of which the pathogen forms biofilms in order to survive the bile. Several genetic components, including the yihU–yshA genes, have been suggested to be involved in the survival of Salmonella in the gallbladder. In this work we describe how the yihU–yshA gene cluster forms a transcriptional unit regulated positively by the cAMP receptor global regulator CRP (cAMP receptor protein). The results obtained show that two CRP-binding sites on the regulatory region of the yihU–yshA operon are required to promote transcriptional activation. In this work we also demonstrate that the yihU–yshA transcriptional unit is carbon catabolite-repressed in Salmonella, indicating that it forms part of the CRP regulon in enteric bacteria.

Influence of RpoS, cAMP-receptor protein, and ppGpp on expression of the opgGH operon and osmoregulated periplasmic glucan content of Salmonella enterica serovar Typhimurium

2009 ◽  
Vol 55 (11) ◽  
pp. 1284-1293 ◽  
Author(s):  
Cristina S. Costa ◽  
Ramón A. Pizarro ◽  
Dora N. Antón
Keyword(s):  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Regulatory System ◽  
Receptor Protein ◽  
Transcriptional Level ◽  
Camp Receptor Protein ◽  
High Osmolarity ◽  
Serovar Typhimurium ◽  
Camp Receptor ◽  
Periplasmic Glucan

A transcriptional fusion (opgG1::MudJ) to the opgGH operon of Salmonella enterica serovar Typhimurium (S. Typhimurium) LT2, isolated by resistance to mecillinam, was used to study the influence of global regulators RpoS, ppGpp, and cAMP/cAMP-receptor protein (CRP) on expression of the opgGH operon and osmoregulated periplasmic glucan (OPG) content. Neither high growth medium osmolarity nor absence of ppGpp or CRP had important effects on opgG1::MudJ expression in exponential cultures. However, under the same conditions, OPG content was strongly decreased by high osmolarity or cAMP/CRP defectiveness, and reduced to a half by lack of ppGpp. In stationary cultures, high osmolarity as well as CRP loss caused significant descents in opgG1::MudJ expression that were compensated by inactivation of RpoS σ factor. No effect of RpoS inactivation on OPG content was observed. It is concluded that opgGH expression in S. Typhimurium is only slightly affected by high osmolarity, but is inversely modulated by RpoS level. On the other hand, osmolarity and the cAMP/CRP global regulatory system appear to control OPG content, either directly or indirectly, mainly at the post-transcriptional level.

scholarly journals cAMP Receptor Protein Positively Regulates the Expression of Genes Involved in the Biosynthesis of Klebsiella oxytoca Tilivalline Cytotoxin

2021 ◽  
Vol 12 ◽  
Author(s):  
Diana Rodríguez-Valverde ◽  
Nancy León-Montes ◽  
Jorge Soria-Bustos ◽  
Jessica Martínez-Cruz ◽  
Ricardo González-Ugalde ◽  
...  
Keyword(s):  
Gene Expression ◽  
Metabolic Regulation ◽  
Divalent Cations ◽  
Klebsiella Oxytoca ◽  
Carbon Sources ◽  
Enteric Bacteria ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Environmental Signals ◽  
Camp Receptor

Klebsiella oxytoca is a resident of the human gut. However, certain K. oxytoca toxigenic strains exist that secrete the nonribosomal peptide tilivalline (TV) cytotoxin. TV is a pyrrolobenzodiazepine that causes antibiotic-associated hemorrhagic colitis (AAHC). The biosynthesis of TV is driven by enzymes encoded by the aroX and NRPS operons. In this study, we determined the effect of environmental signals such as carbon sources, osmolarity, and divalent cations on the transcription of both TV biosynthetic operons. Gene expression was enhanced when bacteria were cultivated in tryptone lactose broth. Glucose, high osmolarity, and depletion of calcium and magnesium diminished gene expression, whereas glycerol increased transcription of both TV biosynthetic operons. The cAMP receptor protein (CRP) is a major transcriptional regulator in bacteria that plays a key role in metabolic regulation. To investigate the role of CRP on the cytotoxicity of K. oxytoca, we compared levels of expression of TV biosynthetic operons and synthesis of TV in wild-type strain MIT 09-7231 and a Δcrp isogenic mutant. In summary, we found that CRP directly activates the transcription of the aroX and NRPS operons and that the absence of CRP reduced cytotoxicity of K. oxytoca on HeLa cells, due to a significant reduction in TV production. This study highlights the importance of the CRP protein in the regulation of virulence genes in enteric bacteria and broadens our knowledge on the regulatory mechanisms of the TV cytotoxin.

Influence of the Location of the cAMP Receptor Protein Binding Site on the Geometry of a Transcriptional Activation Complex inEscherichiacoli†

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15302-15312 ◽  
Author(s):  
Patrick Eichenberger ◽  
Sylvie Déthiollaz ◽  
Nobuyuki Fujita ◽  
Akira Ishihama ◽  
Johannes Geiselmann
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Transcriptional Activation ◽  
Receptor Protein ◽  
Protein Binding Site ◽  
Camp Receptor Protein ◽  
Camp Receptor

Transcriptional regulation of sdiA by cAMP-receptor protein, LeuO, and environmental signals in Salmonella enterica serovar Typhimurium

2012 ◽  
Vol 58 (1) ◽  
pp. 10-22 ◽  
Author(s):  
Amy L. Turnbull ◽  
Wook Kim ◽  
Michael G. Surette
Keyword(s):  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Late Stationary Phase ◽  
Environmental Signals ◽  
Serovar Typhimurium ◽  
Elevated Expression ◽  
Transcriptional Changes ◽  
Camp Receptor

The sdiA gene encodes for a LuxR-type transcription factor, which is active when bound to N-acyl homoserine lactones (AHLs). Because Salmonella enterica serovar Typhimurium does not produce AHLs, SdiA senses signals produced by other organisms. SdiA is not expressed constitutively, and response is limited to conditions in which elevated expression occurs, but little is known about the regulation of sdiA expression. Here we map the sdiA promoter and define several regulators that directly or indirectly act on the promoter. The major activator of sdiA expression is cAMP-receptor protein (CRP), and we define the CRP operator in the sdiA promoter using promoter and crp mutants. LeuO activates sdiA expression to a lesser extent than does CRP. We demonstrate that LeuO directly binds the sdiA promoter and the Rcs phosphorelay represses sdiA expression. In this study, NhaR, IlvY, and Fur affected sdiA expression indirectly and weakly. Expression in late-stationary phase depended on RpoS. AHL-dependent expression of the SdiA-regulated gene rck correlated to the observed sdiA transcriptional changes in regulator mutants. The data demonstrate that regulation of sdiA involves integration of multiple environmental and metabolic signals.

scholarly journals Expression of the cpdA Gene, Encoding a 3′,5′-Cyclic AMP (cAMP) Phosphodiesterase, Is Positively Regulated by the cAMP-cAMP Receptor Protein Complex

2008 ◽  
Vol 191 (3) ◽  
pp. 922-930 ◽  
Author(s):  
Han-Suk Kim ◽  
Sung-Min Kim ◽  
Hyun-Jung Lee ◽  
Soon-Jung Park ◽  
Kyu-Ho Lee
Keyword(s):  
Regulatory Region ◽  
Site Directed Mutagenesis ◽  
Receptor Protein ◽  
Upstream Region ◽  
Intracellular Camp ◽  
Dependent Manner ◽  
Multicopy Plasmid ◽  
Camp Receptor Protein ◽  
Camp Phosphodiesterase ◽  
Camp Receptor

ABSTRACT The intracellular level of cyclic 3′,5′-AMP (cAMP), a signaling molecule that mediates a variety of cellular processes, is finely modulated by the regulation of its synthesis, excretion, and degradation. In this study, cAMP phosphodiesterase (CpdA), an enzyme that catalyzes the conversion of cAMP to AMP, was characterized in a pathogenic bacterium, Vibrio vulnificus. The cpdA gene exists in an operon composed of mutT, yqiB, cpdA, and yqiA, the transcription of which was initiated at position −22 upstream of mutT. A cpdA-null mutant of V. vulnificus contained significantly higher levels of cAMP than the wild type but showed no detectable cAMP when a multicopy plasmid of the cpdA gene was provided in trans, suggesting that CpdA is responsible for cAMP degradation. Cellular contents of the CpdA protein decreased dramatically in both cya and crp mutants. In addition, levels of expression of the cpdA::luxAB transcription fusion decreased in cya and crp mutants. The level of expression of cpdA::luxAB in the cya mutant increased in a concentration-dependent manner upon the exogenous addition of cAMP. The cAMP-cAMP receptor protein (CRP) complex bound directly to the upstream region of mutT, which includes a putative CRP-binding sequence centered at position −95.5 relative to the transcription start site. Site-directed mutagenesis or the deletion of this sequence in the cpdA::luxAB transcription fusion resulted in the loss of regulation by cAMP and CRP. Thus, this study demonstrates that CpdA plays a crucial role in determining the intracellular cAMP level and shows for the first time that the expression of cpdA is activated by the cAMP-CRP complex via direct binding to the regulatory region.

scholarly journals The yiaKLX1X2PQRS and ulaABCDEFG Gene Systems Are Required for the Aerobic Utilization of l-Ascorbate in Klebsiella pneumoniae Strain 13882 with l-Ascorbate-6-Phosphate as the Inducer

2008 ◽  
Vol 190 (20) ◽  
pp. 6615-6624 ◽  
Author(s):  
Evangelina Campos ◽  
Lucia de la Riva ◽  
Fernando Garces ◽  
Rosa Giménez ◽  
Juan Aguilar ◽  
...  
Keyword(s):  
Klebsiella Pneumoniae ◽  
Genetic System ◽  
Enteric Bacteria ◽  
Metabolic Process ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Phosphotransferase System ◽  
Present Evidence ◽  
Aerobic Conditions ◽  
Camp Receptor

ABSTRACT The capacity to both ferment and oxidize l-ascorbate has been widely documented for a number of enteric bacteria. Here we present evidence that all the strains of Klebsiella pneumoniae tested in this study ferment l-ascorbate using the ula regulon-encoded proteins. Under aerobic conditions, several phenotypes were observed for the strains. Our results showed that the yiaK-S system is required for this aerobic metabolic process. Gel shift experiments performed with UlaR and YiaJ and probes corresponding to the specific promoters indicated that l-ascorbate-6-phosphate is the effector molecule recognized by both regulators, since binding of the repressors to their recognition sites was impaired by the presence of this compound. We demonstrated that in K. pneumoniae cells l-ascorbate-6-phosphate is formed only by the action of the UlaABC phosphotransferase system. This finding explains why strains that lack the ula genetic system and therefore are unable to form the inducer intracellularly cannot efficiently use this vitamin as a carbon source under either anaerobic or aerobic conditions. Thus, efficient aerobic metabolism of l-ascorbate in K. pneumoniae is dependent on the presence of both the yiaK-S and ula systems. The expression of the yiaK-S operon, but not the expression of the ula regulon, is controlled by oxygen availability. Both systems are regulated by the cyclic AMP (cAMP)-cAMP receptor protein (CRP) complex and by IHF.

scholarly journals The cAMP receptor protein of Trypanosoma cruzi.

1983 ◽  
Vol 258 (11) ◽  
pp. 6979-6983 ◽  
Author(s):  
R Rangel-Aldao ◽  
G Tovar ◽  
M Ledezma de Ruiz
Keyword(s):  
Trypanosoma Cruzi ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Camp Receptor
Sign in / Sign up

Export Citation Format

Share Document