Comparison of the PR mutant with the wild-type strain ofProteus mirabilisbrings insight into peroxide resistance factors and regulation of catalase expression

2001 ◽  
Vol 47 (2) ◽  
pp. 130-138 ◽  
Author(s):  
Pierre Andreoletti ◽  
Bruno Franzetti ◽  
Laurent Nussaume ◽  
Jean-Pierre Andrieu ◽  
Jean Gagnon ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Proteus Mirabilis ◽  
Resistant Mutant ◽  
Wild Type ◽  
Resistance Factors ◽  
Alkyl Hydroperoxide ◽  
In The Wild ◽  
Large Production ◽  
Flanking Regions ◽  
Insight Into

The peroxide resistant mutant (PR) of Proteus mirabilis was characterized by an increased constitutive catalase activity concomitant with a large production of specific mRNA. Survival toward hydrogen peroxide during exponential phase was increased by H2O2pretreatment in the wild type but not in the mutant, although the catalase of both strains was not inducible under these conditions. In the mutant, besides catalase, over-produced proteins comprised two different alkyl hydroperoxide reductase subunit C (AhpC) proteins and a protein homologous to the stationary phase transcription factor SspA of Escherichia coli. Conversely, the flagellin A (FlaA) of P. mirabilis was repressed in the PR mutant. Genomic DNA fragments of 2.9 kb carrying the catalase gene (katA) together with the 5' and 3' flanking regions were isolated from both strains and found to be identical. Upstream of katA, a Fur box-like sequence was found, but surprisingly, restricting iron in the culture medium caused a decrease in catalase production. The PR mutant presents similarities with other peroxide resistant mutants, but the regulation of catalase biosynthesis in P. mirabilis seems somewhat different from other close species such as E. coli.Key words: Proteus mirabilis, hydrogen peroxide, peroxide resistant mutant, catalase.

Comparison of the PR mutant with the wild-type strain of Proteus mirabilis brings insight into peroxide resistance factors and regulation of catalase expression

2001 ◽  
Vol 47 (2) ◽  
pp. 130-138 ◽  
Author(s):  
Pierre Andreoletti ◽  
Bruno Franzetti ◽  
Laurent Nussaume ◽  
Jean-Pierre Andrieu ◽  
Jean Gagnon ◽  
...  
Keyword(s):  
Proteus Mirabilis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Wild Type ◽  
Resistance Factors ◽  
Insight Into

Propriétés d'un mutant de Proteus mirabilis résistant au peroxyde d'hydrogène

1979 ◽  
Vol 25 (3) ◽  
pp. 312-320 ◽  
Author(s):  
G. Sauret ◽  
H. Jouve ◽  
J. Pelmont
Keyword(s):  
Hydrogen Peroxide ◽  
Proteus Mirabilis ◽  
Resistant Mutant ◽  
Wild Type ◽  
Membrane Enzyme ◽  
Internal Membrane ◽  
Mutagenic Property ◽  
High Doses

A peroxide-resistant mutant (PR) was isolated from Proteus mirabilis using the hydrogen peroxide mutagenic property. Under the same conditions, resistance of mutant PR bacteria to H2O2 was 50 to 100 times greater than that of the wild type. The total amount of catalase produced by P. mirabilis PR was on the average 10 times greater than that of the wild type. When PR bacteria were subjected to high doses of H2O2 (150 mM), the determination of catalasic activity in vivo increased; paradoxically, there was a net decrease in the activity of the solubilized catalase after the breakdown of the cells. The hypothesis of an enzyme transfer from the inside towards the periphery of the cells is discussed. The behavior of a membrane enzyme (L-phenylalanine oxidase) of the PR mutant shows that H2O2 may cause lesions way up to the internal membrane of bacteria.

scholarly journals Escherichia coli MutM Suppresses Illegitimate Recombination Induced by Oxidative Stress

Genetics ◽  
1999 ◽  
Vol 151 (2) ◽  
pp. 439-446 ◽  
Author(s):  
Masaaki Onda ◽  
Katsuhiro Hanada ◽  
Hirokazu Kawachi ◽  
Hideo Ikeda
Keyword(s):  
Oxidative Stress ◽  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Dna Damage ◽  
Double Strand Breaks ◽  
Illegitimate Recombination ◽  
Recombination Analysis ◽  
Wild Type ◽  
Strand Breaks ◽  
In The Wild

Abstract DNA damage by oxidative stress is one of the causes of mutagenesis. However, whether or not DNA damage induces illegitimate recombination has not been determined. To study the effect of oxidative stress on illegitimate recombination, we examined the frequency of λbio transducing phage in the presence of hydrogen peroxide and found that this reagent enhances illegitimate recombination. To clarify the types of illegitimate recombination, we examined the effect of mutations in mutM and related genes on the process. The frequency of λbio transducing phage was 5- to 12-fold higher in the mutM mutant than in the wild type, while the frequency in the mutY and mutT mutants was comparable to that of the wild type. Because 7,8-dihydro-8-oxoguanine (8-oxoG) and formamido pyrimidine (Fapy) lesions can be removed from DNA by MutM protein, these lesions are thought to induce illegitimate recombination. Analysis of recombination junctions showed that the recombination at Hotspot I accounts for 22 or 4% of total λbio transducing phages in the wild type or in the mutM mutant, respectively. The preferential increase of recombination at nonhotspot sites with hydrogen peroxide in the mutM mutant was discussed on the basis of a new model, in which 8-oxoG and/or Fapy residues may introduce double-strand breaks into DNA.

scholarly journals RpoS-Dependent Stress Response and Exoenzyme Production in Vibrio vulnificus

2003 ◽  
Vol 69 (10) ◽  
pp. 6114-6120 ◽  
Author(s):  
A. Hülsmann ◽  
T. M. Rosche ◽  
I.-S. Kong ◽  
H. M. Hassan ◽  
D. M. Beam ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Stress Response ◽  
Mutant Strain ◽  
Environmental Changes ◽  
Vibrio Vulnificus ◽  
High Sensitivity ◽  
Striking Difference ◽  
Wild Type ◽  
Hydrolytic Activities ◽  
In The Wild

ABSTRACT Vibrio vulnificus is an estuarine bacterium capable of causing rapidly fatal infections through both ingestion and wound infection. Like other opportunistic pathogens, V. vulnificus must adapt to potentially stressful environmental changes while living freely in seawater, upon colonization of the oyster gut, and upon infection of such diverse hosts as humans and eels. In order to begin to understand the ability of V. vulnificus to respond to such stresses, we examined the role of the alternate sigma factor RpoS, which is important in stress response and virulence in many pathogens. An rpoS mutant of V. vulnificus strain C7184o was constructed by homologous recombination. The mutant strain exhibited a decreased ability to survive diverse environmental stresses, including exposure to hydrogen peroxide, hyperosmolarity, and acidic conditions. The most striking difference was a high sensitivity of the mutant to hydrogen peroxide. Albuminase, caseinase, and elastase activity were detected in the wild type but not in the mutant strain, and an additional two hydrolytic activities (collagenase and gelatinase) were reduced in the mutant strain compared to the wild type. Additionally, the motility of the rpoS mutant was severely diminished. Overall, these studies suggest that rpoS in V. vulnificus is important for adaptation to environmental changes and may have a role in virulence.

scholarly journals Effects of Chloramphenicol on the Mitochondrial Respiratory Chain in the Wild Strain and in a Cytoplasmic Chloramphenicol-Resistant Mutant ofTetrahymena pyriformis

1982 ◽  
Vol 2 (6) ◽  
pp. 715-719 ◽  
Author(s):  
Roland Perasso ◽  
Jean-Jacques Curgy ◽  
Nicole Stelly ◽  
Jean Andre
Keyword(s):  
Oxygen Consumption ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Wild Strain ◽  
Resistant Mutant ◽  
Wild Type ◽  
Mitochondrial Translation ◽  
Cytochrome Oxidase Activity ◽  
In The Wild ◽  
Mitochondrial Respiratory

The effects of chloramphenicol (CAP) on mitochondrial respiratory activity in the wild strain (ST) and in a cytoplasmic CAP-resistant mutant (STR1) ofTetrahymena pyriformiswere studied by determining oxygen consumption, by spectrophotometry, and by cytochemistry. In the absence of CAP both strains had the same respiration capacity, and the low-temperature spectra of their isolated mitochondria were similar. Furthermore, the mitochondria of both strains showed a positive reaction with diaminobenzidine, denoting a similar cytochrome oxidase activity. However, when cells were grown in CAP for 24 or 48 h, the peaks of cytochrome oxidase and cytochromebwere almost absent in the wild type. In this type the oxygen consumption was greatly decreased, and the mitochondria were no longer stained by diaminobenzidine. In the mutant, the peaks of cytochrome oxidase and cytochromebwere decreased only; respiration was less affected than in the wild type, and cytochrome oxidase activity was still disclosed by the diaminobenzidine reaction. These results show that CAP inhibits the synthesis of two cytochromes (band oxidase) which are partially translated into the mitochrondria ofT. pyriformis.In the mutant, CAP reduces only the mitochondrial translation, resulting in reduced mitochondrial activity and reduced growth rate of the cell. These results are compared with the nucleo-mitochondrial regulation mechanisms discussed in our previous works.

The role of catalase in hydrogen peroxide resistance in fission yeast Schizosaccharomyces pombe

1999 ◽  
Vol 45 (2) ◽  
pp. 125-129 ◽  
Author(s):  
Norihiro Mutoh ◽  
Chiaki W Nakagawa ◽  
Kenichiro Yamada
Keyword(s):  
Hydrogen Peroxide ◽  
Schizosaccharomyces Pombe ◽  
Catalase Activity ◽  
Parent Strain ◽  
Normal Growth ◽  
Wild Type ◽  
Catalase Gene ◽  
In The Wild ◽  
High Concentrations

The role of catalase in hydrogen peroxide resistance in Schizosaccharomyces pombe was investigated. A catalase gene disruptant completely lacking catalase activity is more sensitive to hydrogen peroxide than the parent strain. The mutant does not acquire hydrogen peroxide resistance by osmotic stress, a treatment that induces catalase activity in the wild-type cells. The growth rate of the disruptant is not different from that of the parent strain. Additionally, transformed cells that overexpress the catalase activity are more resistant to hydrogen peroxide than wild-type cells with normal catalase activity. These results indicate that the catalase of S. pombe plays an important role in resistance to high concentrations of hydrogen peroxide but offers little in the way of protection from the hydrogen peroxide generated in small amounts under normal growth conditions.Key words: catalase, gene disruption, induced hydrogen peroxide resistance, overexpression, Schizosaccharomyces pombe.

scholarly journals ISOLATION AND PROPERTIES OF SELENOMETHIONINE-RESISTANT MUTANTS OF NEUROSPORA CRASSA

Genetics ◽  
1974 ◽  
Vol 77 (4) ◽  
pp. 627-638
Author(s):  
Gregory S Chen ◽  
Robert L Metzenberg
Keyword(s):  
Resistant Mutant ◽  
Heat Stability ◽  
Temperature Sensitive ◽  
Wild Type ◽  
High Concentration ◽  
Type Locus ◽  
Group I ◽  
In The Wild ◽  
Resistant Mutants ◽  
Adenosylmethionine Synthetase

ABSTRACT Mutants resistant to selenomethionine were isolated, and their properties studied. Mapping studies indicate that the mutation sites are located near the eth-1r locus in linkage group I, about ten map units away from the mating type locus. The sites of new mutation are either allelic to or very close to eth-1r. They are resistant not only to selenomethionine but also to ethionine, while the ethionine-resistant mutant, eth-1r, is sensitive to selenomethionine. The selenomethionine-resistant mutants are also temperature-sensitive mutants. However, they can grow at higher temperatures in medium containing 1 M glycerol.—It is very unlikely that the resistance is due to a change in the permeability of the membrane. Aryl sulfatase of se-metr mutants is not repressed by a high concentration of methionine (5 mM), although inorganic sulfate (2 mM) still can cause total repression. The γ-cystathionase levels of the mutants are normal, but the S-adenosylmethionine synthetase levels are only one-tenth of that observed in the wild-type strain. The heat-stability of this enzyme in the mutant is also different from that of the wild-type enzyme suggesting that the mutation might affect the structural gene of S-adenosylmethionine synthetase.

scholarly journals Regulation of Hydrogen Peroxide-Dependent Gene Expression in Rhodobacter sphaeroides: Regulatory Functions of OxyR

2007 ◽  
Vol 189 (10) ◽  
pp. 3784-3792 ◽  
Author(s):  
Tanja Zeller ◽  
Mobarak A. Mraheil ◽  
Oleg V. Moskvin ◽  
Kuanyu Li ◽  
Mark Gomelsky ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Rhodobacter Sphaeroides ◽  
Expression Patterns ◽  
Class Iii ◽  
Wild Type ◽  
Binding Studies ◽  
Regulatory Pathways ◽  
Mutant Strains ◽  
In The Wild

ABSTRACT Genome-wide transcriptome profiling was used to reveal hydrogen peroxide (H2O2)-dependent regulatory mechanisms in the facultatively photosynthetic bacterium Rhodobacter sphaeroides. In this study we focused on the role of the OxyR protein, a known regulator of the H2O2 response in bacteria. The transcriptome profiles of R. sphaeroides wild-type and oxyR mutant strains that were exposed to 1 mM H2O2 for 7 min or were not exposed to H2O2 were analyzed. Three classes of OxyR-dependent genes were identified based on their expression patterns in the wild type of oxyR mutant strains with differing predicted roles of oxidized and reduced OxyR as activators of transcription. DNA binding studies revealed that OxyR binds upstream of class I genes, which are induced by H2O2 and exhibit similar basal levels of expression in the wild-type and oxyR mutant strains. The effect of OxyR on class II genes, which are also induced by H2O2 but exhibit significantly lower basal levels of expression in the wild-type strain than in the mutant, is indirect. Interestingly, reduced OxyR also activates expression of few genes (class III). The role of reduced OxyR as an activator is shown for the first time. Our data reveal that the OxyR-mediated response is fast and transient. In addition, we found that additional regulatory pathways are involved in the H2O2 response.

Role of Cu,Zn-SOD in the synthesis of endogenous vasodilator hydrogen peroxide during reactive hyperemia in mouse mesenteric microcirculation in vivo

2008 ◽  
Vol 294 (1) ◽  
pp. H441-H448 ◽  
Author(s):  
Toyotaka Yada ◽  
Hiroaki Shimokawa ◽  
Keiko Morikawa ◽  
Aya Takaki ◽  
Yoshiro Shinozaki ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Reactive Hyperemia ◽  
Fluorescent Microscopy ◽  
Artery Occlusion ◽  
Wild Type ◽  
Charge Coupled Device ◽  
In The Wild ◽  
Mesenteric Microcirculation

We have recently demonstrated that endothelium-derived hydrogen peroxide (H2O2) is an endothelium-derived hyperpolarizing factor and that endothelial Cu/Zn-superoxide dismutase (SOD) plays an important role in the synthesis of endogenous H2O2 in both animals and humans. We examined whether SOD plays a role in the synthesis of endogenous H2O2 during in vivo reactive hyperemia (RH), an important regulatory mechanism. Mesenteric arterioles from wild-type and Cu,Zn-SOD−/− mice were continuously observed by a pencil-type charge-coupled device (CCD) intravital microscope during RH (reperfusion after 20 and 60 s of mesenteric artery occlusion) in the cyclooxygenase blockade under the following four conditions: control, catalase alone, NG-monomethyl-l-arginine (l-NMMA) alone, and l-NMMA + catalase. Vasodilatation during RH was significantly decreased by catalase or l-NMMA alone and was almost completely inhibited by l-NMMA + catalase in wild-type mice, whereas it was inhibited by l-NMMA and l-NMMA + catalase in the Cu,Zn-SOD−/− mice. RH-induced increase in blood flow after l-NMMA was significantly increased in the wild-type mice, whereas it was significantly reduced in the Cu,Zn-SOD−/− mice. In mesenteric arterioles of the Cu,Zn-SOD−/− mice, Tempol, an SOD mimetic, significantly increased the ACh-induced vasodilatation, and the enhancing effect of Tempol was decreased by catalase. Vascular H2O2 production by fluorescent microscopy in mesenteric arterioles after RH was significantly increased in response to ACh in wild-type mice but markedly impaired in Cu,Zn-SOD−/− mice. Endothelial Cu,Zn-SOD plays an important role in the synthesis of endogenous H2O2 that contributes to RH in mouse mesenteric smaller arterioles.

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