scholarly journals Involvement of ResE Phosphatase Activity in Down-Regulation of ResD-Controlled Genes in Bacillus subtilis during Aerobic Growth

2001 ◽  
Vol 183 (6) ◽  
pp. 1938-1944 ◽  
Author(s):  
Michiko M. Nakano ◽  
Yi Zhu
Keyword(s):  
Bacillus Subtilis ◽  
Phosphatase Activity ◽  
Response Regulator ◽  
Anaerobic Respiration ◽  
Signal Transduction System ◽  
Aerobic Growth ◽  
High Level ◽  
Histidine Sensor Kinase ◽  
Cognate Response Regulator ◽  
Aerobic And Anaerobic

ABSTRACT The ResD-ResE signal transduction system is required for aerobic and anaerobic respiration in Bacillus subtilis. The histidine sensor kinase ResE, by functioning as a kinase and a phosphatase for the cognate response regulator ResD, controls the level of phosphorylated ResD. A high level of phosphorylated ResD is postulated to cause a dramatic increase in transcription of ResDE-controlled genes under anaerobic conditions. A mutant ResE, which retains autophosphorylation and ResD phosphorylation activities but is defective in ResD dephosphorylation, allowed partially derepressed aerobic expression of the ResDE-controlled genes. The result indicates that phosphatase activity of ResE is regulated by oxygen availability and anaerobic induction of the ResDE regulon is partly due to a reduction of the ResE phosphatase activity during anaerobiosis. That elimination of phosphatase activity does not result in complete aerobic derepression suggests that the ResE kinase activity is also subject to control in response to oxygen limitation.

scholarly journals RegB/RegA, a Highly Conserved Redox-Responding Global Two-Component Regulatory System

2004 ◽  
Vol 68 (2) ◽  
pp. 263-279 ◽  
Author(s):  
Sylvie Elsen ◽  
Lee R. Swem ◽  
Danielle L. Swem ◽  
Carl E. Bauer
Keyword(s):  
Carbon Fixation ◽  
Rhodobacter Capsulatus ◽  
Response Regulator ◽  
Bacterial Species ◽  
Anaerobic Respiration ◽  
Regulatory System ◽  
Redox Active ◽  
Membrane Bound ◽  
Cognate Response Regulator ◽  
Aerobic And Anaerobic

SUMMARY The Reg regulon from Rhodobacter capsulatus and Rhodobacter sphaeroides encodes proteins involved in numerous energy-generating and energy-utilizing processes such as photosynthesis, carbon fixation, nitrogen fixation, hydrogen utilization, aerobic and anaerobic respiration, denitrification, electron transport, and aerotaxis. The redox signal that is detected by the membrane-bound sensor kinase, RegB, appears to originate from the aerobic respiratory chain, given that mutations in cytochrome c oxidase result in constitutive RegB autophosphorylation. Regulation of RegB autophosphorylation also involves a redox-active cysteine that is present in the cytosolic region of RegB. Both phosphorylated and unphosphorylated forms of the cognate response regulator RegA are capable of activating or repressing a variety of genes in the regulon. Highly conserved homologues of RegB and RegA have been found in a wide number of photosynthetic and nonphotosynthetic bacteria, with evidence suggesting that RegB/RegA plays a fundamental role in the transcription of redox-regulated genes in many bacterial species.

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 A Mutation in the 3-Phosphoglycerate Kinase Gene Allows Anaerobic Growth of Bacillus subtilis in the Absence of ResE Kinase

1999 ◽  
Vol 181 (22) ◽  
pp. 7087-7097 ◽  
Author(s):  
Michiko M. Nakano ◽  
Yi Zhu ◽  
Koki Haga ◽  
Hirofumi Yoshikawa ◽  
Abraham L. Sonenshein ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Response Regulator ◽  
Anaerobic Respiration ◽  
Phosphoglycerate Kinase ◽  
Anaerobic Growth ◽  
Wild Type ◽  
Kinase Gene ◽  
Glycolytic Intermediate

ABSTRACT The Bacillus subtilis ResD-ResE two-component signal transduction system is essential for aerobic and anaerobic respiration. A spontaneous suppressor mutant that expresses ResD-controlled genes and grows anaerobically in the absence of the ResE histidine kinase was isolated. In addition, aerobic expression of ResD-controlled genes in the suppressed strain was constitutive and occurred at a much higher level than that observed in the wild-type strain. The suppressing mutation, which mapped to pgk, the gene encoding 3-phosphoglycerate kinase, failed to suppress a resDmutation, suggesting that the suppressing mutation creates a pathway for phosphorylation of the response regulator, ResD, which is independent of the cognate sensor kinase, ResE. The pgk-1mutant exhibited very low but measurable 3-phosphoglycerate kinase activity compared to the wild-type strain. The results suggest that accumulation of a glycolytic intermediate, probably 1,3-diphosphoglycerate, is responsible for the observed effect of thepgk-1 mutation on anaerobiosis of resE mutant cells.

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 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 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.

scholarly journals The CpxRA Signal Transduction System ofEscherichia coli: Growth-Related Autoactivation and Control of Unanticipated Target Operons

1999 ◽  
Vol 181 (21) ◽  
pp. 6772-6778 ◽  
Author(s):  
Peter De Wulf ◽  
Ohsuk Kwon ◽  
E. C. C. Lin
Keyword(s):  
Signal Transduction ◽  
Response Regulator ◽  
Consensus Sequence ◽  
Negative Control ◽  
Northern Hybridization ◽  
Signal Transduction System ◽  
Mobility Shift ◽  
Response Network ◽  
Shift Analysis ◽  
Cognate Response Regulator

ABSTRACT In Escherichia coli, the CpxRA two-component signal transduction system senses and responds to aggregated and misfolded proteins in the bacterial envelope. We show that CpxR-P (the phosphorylated form of the cognate response regulator) activatescpxRA expression in conjunction with RpoS, suggesting an involvement of the Cpx system in stationary-phase survival. Engagement of the CpxRA system in functions beyond protein management is indicated by several putative targets identified after a genomic screening for the CpxR-P recognition consensus sequence. Direct negative control of the newly identified targets motABcheAW (specifying motility and chemotaxis) and tsr (encoding the serine chemoreceptor) by CpxR-P was shown by electrophoretic mobility shift analysis and Northern hybridization. The results suggest that the CpxRA system plays a core role in an extensive stress response network in which the coordination of protein turnover and energy conservation may be the unifying element.

scholarly journals Cysteine-Scanning Analysis of the Dimerization Domain of EnvZ, an Osmosensing Histidine Kinase

2003 ◽  
Vol 185 (11) ◽  
pp. 3429-3435 ◽  
Author(s):  
Ling Qin ◽  
Shengjian Cai ◽  
Yan Zhu ◽  
Masayori Inouye
Keyword(s):  
Phosphatase Activity ◽  
Response Regulator ◽  
Phosphorylation Site ◽  
Dimerization Domain ◽  
Phosphatase Domain ◽  
Mutant Proteins ◽  
Cysteine Scanning ◽  
Substitution Mutations ◽  
Cognate Response Regulator

ABSTRACT EnvZ and OmpR are a transmembrane sensor and its cognate response regulator, respectively, regulating the transcription of porin genes in response to medium osmolarity in Escherichia coli. The cytoplasmic domain of EnvZ (EnvZc) possesses both kinase and phosphatase activities and can be dissected into two functional domains, A and B. Here, we performed a cysteine-scanning analysis of domain A, a 67-residue central dimerization and phosphatase domain containing His-243 as the phosphorylation site, and we examined the effects of the cysteine substitution mutations on the enzymatic activities of domain A. The substitution mutations were made at 31 residues, from which 24 mutant domain A proteins were biochemically characterized. From the analysis of the phosphatase activity of purified mutant proteins, it was found that there are two regions in domain A which are important for this activity. Cysteine mutations in these regions dramatically reduce or completely abolish the phosphatase activity of domain A. The mutations that have the most-severe effects on domain A phosphatase activity also significantly reduce the phosphatase activity of EnvZc containing the same mutation. Using an in vitro complementation system with EnvZc(H243V), these cysteine mutants were further characterized for their autophosphorylation activities as well as their phosphotransfer activities. The results indicate that some mutations are specific either for the phosphatase activity or for the kinase activity.

scholarly journals High- and Low-Threshold Genes in the Spo0A Regulon of Bacillus subtilis

2005 ◽  
Vol 187 (4) ◽  
pp. 1357-1368 ◽  
Author(s):  
Masaya Fujita ◽  
José Eduardo González-Pastor ◽  
Richard Losick
Keyword(s):  
Bacillus Subtilis ◽  
Low Dose ◽  
Response Regulator ◽  
Regulatory Protein ◽  
Binding Constants ◽  
Threshold Level ◽  
High Threshold ◽  
High Dose ◽  
Direct Role ◽  
High Level

ABSTRACT The master regulator for entry into sporulation in Bacillus subtilis is the response regulator Spo0A, which directly governs the expression of about 121 genes. Using cells in which the synthesis of Spo0A was under the control of an inducible promoter or in which production of the regulatory protein was impaired by a promoter mutation, we found that sporulation required a high (threshold) level of Spo0A and that many genes in the regulon differentially responded to high and low doses of the regulator. We distinguished four categories of genes, as follows: (i) those that required a high level of Spo0A to be activated, (ii) those that required a high level of Spo0A to be repressed, (iii) those that were activated at a low level of the regulator, and (iv) those that were repressed at a low dose of the regulator. Genes that required a high dose of Spo0A to be activated were found to have low binding constants for the DNA-binding protein. Some genes that were turned on at a low dose of Spo0A either had a high binding constant for the regulatory protein or were activated by an indirect mechanism involving Spo0A-mediated relief of repression by the repressor protein AbrB. We propose that progressive increases in the level of Spo0A leads to an early phase of transcription in which genes that play auxiliary roles in development, such as cannibalism and biofilm formation, are turned on and a later phase in which genes that play a direct role in sporulation are activated.

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