Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis

1996 ◽  
Vol 19 (6) ◽  
pp. 1151-1157 ◽  
Author(s):  
Marta Perego ◽  
Philippe Glaser ◽  
James A. Hoch
Keyword(s):  
Signal Transduction ◽  
Bacillus Subtilis ◽  
Response Regulator ◽  
Signal Transduction System

scholarly journals CheX in the Three-Phosphatase System of Bacterial Chemotaxis

2007 ◽  
Vol 189 (19) ◽  
pp. 7007-7013 ◽  
Author(s):  
Travis J. Muff ◽  
Richard M. Foster ◽  
Peter J. Y. Liu ◽  
George W. Ordal
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Bacillus Subtilis ◽  
Mutant Strain ◽  
Response Regulator ◽  
Bacterial Chemotaxis ◽  
Signal Transduction System ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Phosphatase System

ABSTRACT Bacterial chemotaxis involves the regulation of motility by a modified two-component signal transduction system. In Escherichia coli, CheZ is the phosphatase of the response regulator CheY but many other bacteria, including Bacillus subtilis, use members of the CheC-FliY-CheX family for this purpose. While Bacillus subtilis has only CheC and FliY, many systems also have CheX. The effect of this three-phosphatase system on chemotaxis has not been studied previously. CheX was shown to be a stronger CheY-P phosphatase than either CheC or FliY. In Bacillus subtilis, a cheC mutant strain was nearly complemented by heterologous cheX expression. CheX was shown to overcome the ΔcheC adaptational defect but also generally lowered the counterclockwise flagellar rotational bias. The effect on rotational bias suggests that CheX reduced the overall levels of CheY-P in the cell and did not truly replicate the adaptational effects of CheC. Thus, CheX is not functionally redundant to CheC and, as outlined in the discussion, may be more analogous to CheZ.

scholarly journals Resistance to Bacitracin in Bacillus subtilis: Unexpected Requirement of the BceAB ABC Transporter in the Control of Expression of Its Own Structural Genes

2007 ◽  
Vol 189 (23) ◽  
pp. 8636-8642 ◽  
Author(s):  
Remi Bernard ◽  
Annick Guiseppi ◽  
Marc Chippaux ◽  
Maryline Foglino ◽  
François Denizot
Keyword(s):  
Signal Transduction ◽  
Bacillus Subtilis ◽  
Abc Transporter ◽  
Defense Mechanism ◽  
Response Regulator ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Signal Transduction System ◽  
Native Form

ABSTRACT The Bacillus subtilis BceAB ABC transporter involved in a defense mechanism against bacitracin is composed of a membrane-spanning domain and a nucleotide-binding domain. Induction of the structural bceAB genes requires the BceR response regulator and the BceS histidine kinase of a signal transduction system. However, despite the presence of such a transduction system and of bacitracin, no transcription from an unaltered bceA promoter is observed in cells lacking the BceAB transporter. Expression in trans of the BceAB transporter in these bceAB cells restores the transcription from the bceA promoter. Cells possessing a mutated nucleotide-binding domain of the transporter are also no longer able to trigger transcription from the bceA promoter in the presence of bacitracin, although the mutated ABC transporter is still bound to the membrane. In these cells, expression of the bceA promoter can no longer be detected, indicating that the ABC transporter not only must be present in the cell membrane, but also must be expressed in a native form for the induction of the bceAB genes. Several hypotheses are discussed to explain the simultaneous need for bacitracin, a native signal transduction system, and an active BceAB ABC transporter to trigger transcription from the bceA promoter.

scholarly journals Multistress Regulation in Escherichia coli: Expression of osmB Involves Two Independent Promoters Responding either to σS or to the RcsCDB His-Asp Phosphorelay

2005 ◽  
Vol 187 (9) ◽  
pp. 3282-3286 ◽  
Author(s):  
Alice Boulanger ◽  
Anne Francez-Charlot ◽  
Annie Conter ◽  
Marie-Pierre Castanié-Cornet ◽  
Kaymeuang Cam ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Transcription Factors ◽  
Response Regulator ◽  
Osmotic Shock ◽  
Dependent Manner ◽  
Signal Transduction System ◽  
Upstream Promoter ◽  
Site Consensus ◽  
Escherichia Coli Expression

ABSTRACT Transcription of the Escherichia coli osmB gene is induced by several stress conditions. osmB is expressed from two promoters, osmBp1 and osmBp2. The downstream promoter, osmBp2, is induced after osmotic shock or upon entry into stationary phase in a σS-dependent manner. The upstream promoter, osmBp1, is independent of σS and is activated by RcsB, the response regulator of the His-Asp phosphorelay signal transduction system RcsCDB. RcsB is responsible for the induction of osmBp1 following treatment with chlorpromazine. Activation of osmBp1 by RcsB requires a sequence upstream of its −35 element similar to the RcsB binding site consensus, suggesting a direct regulatory role. osmB appears as another example of a multistress-responsive gene whose transcription involves both a σS-dependent promoter and a second one independent of σS but controlled by stress-specific transcription factors.

scholarly journals Analysis of a Heme-Dependent Signal Transduction System in Corynebacterium diphtheriae: Deletion of the chrAS Genes Results in Heme Sensitivity and Diminished Heme-Dependent Activation of the hmuO Promoter

2005 ◽  
Vol 73 (11) ◽  
pp. 7406-7412 ◽  
Author(s):  
Lori A. Bibb ◽  
Natalie D. King ◽  
Carey A. Kunkle ◽  
Michael P. Schmitt
Keyword(s):  
Signal Transduction ◽  
Transcriptional Activation ◽  
Transcriptional Activity ◽  
Response Regulator ◽  
Corynebacterium Diphtheriae ◽  
Transcriptional Analysis ◽  
Sensor Kinase ◽  
Signal Transduction System ◽  
Dependent Signal ◽  
Two Component Signal Transduction

ABSTRACT The Corynebacterium diphtheriae hmuO gene encodes a heme oxygenase that is involved in the utilization of heme as an iron source. Transcription of hmuO is activated by heme or hemoglobin and repressed by iron and DtxR. Previous studies with Escherichia coli showed that heme-dependent transcriptional activation of an hmuO promoter-lacZ fusion was dependent on the cloned C. diphtheriae chrA and chrS genes (chrAS), which encode the response regulator and sensor kinase, respectively, of a two-component signal transduction system. In this study, nonpolar deletions in the chrAS genes were constructed on the chromosome of C. diphtheriae. Mutations in chrAS resulted in marked reduction in heme-dependent transcription of hmuO, which indicates that the ChrA/S system is a key regulator at the hmuO promoter. However, low but significant levels of heme-specific transcriptional activity were observed at the hmuO promoter in the chrAS mutants, suggesting that an additional heme-dependent activator is involved in hmuO expression. The chrAS mutants were also sensitive to heme, which was observed only in stationary-phase cultures and correlated with reduced cell viability. The heme sensitivity of the mutants was not due to reduced expression of hmuO, and these results suggest that additional factors controlled by the ChrA/S system may be involved in protection against heme toxicity. Transcriptional analysis of the chrAS operon revealed that it was not autoregulated or affected by iron or heme levels.

Phosphorylation activity of the response regulator of the two-component signal transduction system AtoS–AtoC in E. coli

2005 ◽  
Vol 1725 (3) ◽  
pp. 257-268 ◽  
Author(s):  
Efthimia E. Lioliou ◽  
Eleni P. Mimitou ◽  
Asterios I. Grigoroudis ◽  
Cynthia H. Panagiotidis ◽  
Christos A. Panagiotidis ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Response Regulator ◽  
Signal Transduction System ◽  
E Coli ◽  
Two Component ◽  
Two Component Signal Transduction

scholarly journals Rap Phosphatase of Virulence Plasmid pXO1 Inhibits Bacillus anthracis Sporulation

2006 ◽  
Vol 188 (2) ◽  
pp. 487-498 ◽  
Author(s):  
Cristina Bongiorni ◽  
Ricarda Stoessel ◽  
Dorinda Shoemaker ◽  
Marta Perego
Keyword(s):  
Cell Cycle ◽  
Signal Transduction ◽  
Bacillus Anthracis ◽  
Response Regulator ◽  
Selective Advantage ◽  
Virulence Plasmid ◽  
Signal Transduction System ◽  
Developmental Pathway ◽  
Sporulation Initiation ◽  
Carboxy Terminal

ABSTRACT This study shows that the Bacillus anthracis pXO1 virulence plasmid carries a Rap-Phr system, BXA0205, which regulates sporulation initiation in this organism. The BXA0205Rap protein was shown to dephosphorylate the Spo0F response regulator intermediate of the phosphorelay signal transduction system that regulates the initiation of the developmental pathway in response to environmental, metabolic, and cell cycle signals. The activity of the Rap protein was shown to be inhibited by the carboxy-terminal pentapeptide generated through an export-import processing pathway from the associated BXA0205Phr protein. Deregulation of the Rap activity by either overexpression or lack of the Phr pentapeptide resulted in severe inhibition of sporulation. Five additional Rap-Phr encoding systems were identified on the chromosome of B. anthracis, one of which, BA3790-3791, also affected sporulation initiation. The results suggest that the plasmid-borne Rap-Phr system may provide a selective advantage to the virulence of B. anthracis.

scholarly journals Cpx Two-Component Signal Transduction inEscherichia coli: Excessive CpxR-P Levels Underlie CpxA* Phenotypes

2000 ◽  
Vol 182 (5) ◽  
pp. 1423-1426 ◽  
Author(s):  
Peter De Wulf ◽  
E. C. C. Lin
Keyword(s):  
Signal Transduction ◽  
Response Regulator ◽  
Response Regulators ◽  
Signal Transduction System ◽  
Regulate Gene Expression ◽  
Adverse Conditions ◽  
Two Component ◽  
Sensor Protein ◽  
Two Component Signal Transduction ◽  
Cognate Response Regulator

ABSTRACT In Escherichia coli, the CpxA-CpxR two-component signal transduction system and the ςE and ς32response pathways jointly regulate gene expression in adaptation to adverse conditions. These include envelope protein distress, heat shock, oxidative stress, high pH, and entry into stationary phase. Certain mutant versions of the CpxA sensor protein (CpxA* proteins) exhibit an elevated ratio of kinase to phosphatase activity on CpxR, the cognate response regulator. As a result, CpxA* strains display numerous phenotypes, many of which cannot be easily related to currently known functions of the CpxA-CpxR pathway. It is unclear whether CpxA* phenotypes are caused solely by hyperphosphorylation of CpxR. We here report that all of the tested CpxA* phenotypes depend on elevated levels of CpxR-P and not on cross-signalling of CpxA* to noncognate response regulators.

scholarly journals The LisRK Signal Transduction System Determines the Sensitivity of Listeria monocytogenes to Nisin and Cephalosporins

2002 ◽  
Vol 46 (9) ◽  
pp. 2784-2790 ◽  
Author(s):  
Paul D. Cotter ◽  
Caitriona M. Guinane ◽  
Colin Hill
Keyword(s):  
Signal Transduction ◽  
Listeria Monocytogenes ◽  
Histidine Kinase ◽  
Antimicrobial Agents ◽  
Response Regulator ◽  
Signal Transduction System ◽  
Enhanced Sensitivity ◽  
Virulence Potential ◽  
Two Component Signal Transduction

ABSTRACT The Listeria monocytogenes two-component signal transduction system, LisRK, initially identified in strain LO28, plays a significant role in the virulence potential of this important food-borne pathogen. Here, it is shown that, in addition to its major contribution in responding to ethanol, pH, and hydrogen peroxide stresses, LisRK is involved in the ability of the cell to tolerate important antimicrobials used in food and in medicine, e.g., the lantibiotic nisin and the cephalosporin family of antibiotics. A ΔlisK mutant (lacking the LisK histidine kinase sensor component) displays significantly enhanced resistance to the lantibiotic nisin, a greatly enhanced sensitivity to the cephalosporins, and a large reduction in the expression of three genes thought to encode a penicillin-binding protein, another histidine kinase (other than LisK), and a protein of unknown function. Confirmation of the role of LisRK was obtained when the response regulator, LisR, was overexpressed using both constitutive and inducible (nisin-controlled expression) systems. Under these conditions we observed a reversion of the ΔlisK mutant to wild-type growth kinetics in the presence of nisin. It was also found that overexpression of LisR complemented the reduced expression of two of the aforementioned genes. These results demonstrate the important role of LisRK in the response of L. monocytogenes to a number of antimicrobial agents.

scholarly journals Development and Validation of a High-Throughput Cell-Based Screen To Identify Activators of a Bacterial Two-Component Signal Transduction System

2015 ◽  
Vol 59 (7) ◽  
pp. 3789-3799 ◽  
Author(s):  
Julia J. van Rensburg ◽  
Kate R. Fortney ◽  
Lan Chen ◽  
Andrew J. Krieger ◽  
Bruno P. Lima ◽  
...  
Keyword(s):  
Signal Transduction ◽  
High Throughput ◽  
Response Regulator ◽  
Phosphoryl Group ◽  
Signal Transduction System ◽  
Membrane Repair ◽  
Content Type ◽  
Two Component ◽  
Serovar Typhimurium ◽  
Two Component Signal Transduction

ABSTRACTCpxRA is a two-component signal transduction system (2CSTS) found in many drug-resistant Gram-negative bacteria. In response to periplasmic stress, CpxA autophosphorylates and donates a phosphoryl group to its cognate response regulator, CpxR. Phosphorylated CpxR (CpxR-P) upregulates genes involved in membrane repair and downregulates multiple genes that encode virulence factors, which are trafficked across the cell membrane. Mutants that constitutively activate CpxRA inSalmonella entericaserovar Typhimurium andHaemophilus ducreyiare avirulent in mice and humans, respectively. Thus, the activation of CpxRA has high potential as a novel antimicrobial/antivirulence strategy. Using a series ofEscherichia colistrains containing a CpxR-P-responsivelacZreporter and deletions in genes encoding CpxRA system components, we developed and validated a novel cell-based high-throughput screen (HTS) for CpxRA activators. A screen of 36,000 compounds yielded one hit compound that increased reporter activity in wild-type cells. This is the first report of a compound that activates, rather than inhibits, a 2CSTS. The activity profile of the compound against CpxRA pathway mutants in the presence of glucose suggested that the compound inhibits CpxA phosphatase activity. We confirmed that the compound induced the accumulation of CpxR-P in treated cells. Although the hit compound contained a nitro group, a derivative lacking this group retained activity in serum and had lower cytotoxicity than that of the initial hit. This HTS is amenable for the screening of larger libraries to find compounds that activate CpxRA by other mechanisms, and it could be adapted to find activators of other two-component systems.

scholarly journals A Two-Component Signal Transduction System Essential for Growth of Bacillus subtilis: Implications for Anti-Infective Therapy

1998 ◽  
Vol 180 (23) ◽  
pp. 6375-6383 ◽  
Author(s):  
Céline Fabret ◽  
James A. Hoch
Keyword(s):  
Signal Transduction ◽  
Response Regulator ◽  
Temperature Sensitive ◽  
Protease Gene ◽  
Signal Transduction System ◽  
Insertional Inactivation ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
High Level ◽  
Promoter Studies

ABSTRACT A two-component signal transduction system encoded by theyycF and yycG genes is part of an operon containing three genes, yycH, yycI, andyycJ, with no known function and a gene, yycK, coding for an HtrA-like protease. This operon was transcribed during growth, and its transcription shut down as the cells approached stationary phase. This decreased transcription was not Spo0A dependent. The HtrA protease gene was separately controlled during sporulation from a ςG promoter. Studies using insertional inactivation plasmids revealed that neither yycF noryycG could be inactivated, whereas the other genes were inactivated without loss of viability. A temperature-sensitive YycF response regulator mutant was isolated and shown to have an H215P mutation in a putative DNA-binding domain which is closely related to the OmpR family of response regulators. At the nonpermissive temperature, cultures of the mutant strain stopped growth within 30 min, and this was followed by a decrease in optical density. Microscopically, many of the cells appeared to retain their structure while being empty of their contents. The essential processes regulated by this two-component system remain unknown. A search of the genome databases revealed YycF, YycG, and YycJ homologues encoded by three linked genes in Streptococcus pyogenes. The high level of identity of these proteins (71% for YycF) suggests that this system may play a similar role in gram-positive pathogens.

Sign in / Sign up

Export Citation Format

Share Document