Mutation of cytochrome<i>bd</i>quinol oxidase results in reduced stationary phase survival, iron deprivation, metal toxicity and oxidative stress in<i>Azotobacter vinelandii</i>

Edwards, Sian; Loder, Caroline; Wu, Guanghui; Corker, Hazel; Bainbridge, Brian W.; Hill, Susan; Poole, Robert K.

doi:10.1111/j.1574-6968.2000.tb09042.x

Cited by 38 publications

(11 citation statements)

References 28 publications

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“…Disruption of cytochrome bd oxidase increases sensitivity to the respiratory chain inhibitor sodium azide and the uncoupling agent nickel in both Brucella and E. coli (Wall et al, 1992; Edwards et al, 2000; Endley et al, 2001). Similarly to the B. abortus cydB mutant, the mutant lacking cydX was highly sensitive to the combination of sodium azide plus nickel sulfate, compared to wild type B. abortus (Figure 2E).…”

Section: Resultsmentioning

confidence: 99%

The small protein CydX is required for function of cytochrome bd oxidase in Brucella abortus

Sun

Jong

Hartigh

et al. 2012

Front. Cell. Inf. Microbio.

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A large number of hypothetical genes potentially encoding small proteins of unknown function are annotated in the Brucella abortus genome. Individual deletion of 30 of these genes identified four mutants, in BAB1_0355, BAB2_0726, BAB2_0470, and BAB2_0450 that were highly attenuated for infection. BAB2_0726, an YbgT-family protein located at the 3′ end of the cydAB genes encoding cytochrome bd ubiquinal oxidase, was designated cydX. A B. abortus cydX mutant lacked cytochrome bd oxidase activity, as shown by increased sensitivity to H2O2, decreased acid tolerance and increased resistance to killing by respiratory inhibitors. The C terminus, but not the N terminus, of CydX was located in the periplasm, suggesting that CydX is an integral cytoplasmic membrane protein. Phenotypic analysis of the cydX mutant, therefore, suggested that CydX is required for full function of cytochrome bd oxidase, possibly via regulation of its assembly or activity.

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Section: Resultsmentioning

confidence: 99%

The small protein CydX is required for function of cytochrome bd oxidase in Brucella abortus

Sun

Jong

Hartigh

et al. 2012

Front. Cell. Inf. Microbio.

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“…Cytochrome bd oxidase performs a variety of physiological functions in prokaryotes, such as energy-transducing respiration, aerotolerant nitrogen fixation, and protection against metal toxicity and oxidative stress (50)(51)(52)(53)(54). This enzyme has also been implicated in the virulence of Shigella flexneri and several S. enterica serovars such as Typhimurium, Gallinarum, and Dublin (55), suggesting that cytochrome bd may be particularly important for the growth and survival of pathogens that encounter environments in which O 2 is progressively limited.…”

Section: Resultsmentioning

confidence: 99%

RNA Sequencing Reveals Differences between the Global Transcriptomes of Salmonella enterica Serovar Enteritidis Strains with High and Low Pathogenicities

Shah

2014

Appl Environ Microbiol

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Salmonella enterica serovar Enteritidis is one of the important causes of bacterial food-borne gastroenteritis worldwide. Field strains of S. Enteritidis are relatively genetically homogeneous; however, they show extensive phenotypic diversity and differences in virulence potential. RNA sequencing (RNA-Seq) was used to characterize differences in the global transcriptome between several genetically similar but phenotypically diverse poultry-associated field strains of S. Enteritidis grown in laboratory medium at avian body temperature (42°C). These S. Enteritidis strains were previously characterized as high-pathogenicity (HP; n ‫؍‬ 3) and low-pathogenicity (LP; n ‫؍‬ 3) strains based on both in vitro and in vivo virulence assays. Using the negative binomial distribution-based statistical tools edgeR and DESeq, 252 genes were identified as differentially expressed in LP strains compared with their expression in the HP strains (P < 0.05). A majority of genes (235, or 93.2%) showed significantly reduced expression, whereas a few genes (17, or 6.8%) showed increased expression in all LP strains compared with HP strains. LP strains showed a unique transcriptional profile that is characterized by significantly reduced expression of several transcriptional regulators and reduced expression of genes involved in virulence (e.g., Salmonella pathogenicity island 1 [SPI-1], SPI-5, and fimbrial and motility genes) and protection against osmotic, oxidative, and other stresses, such as iron-limiting conditions commonly encountered within the host. Several functionally uncharacterized genes also showed reduced expression. This study provides a first concise view of the global transcriptional differences between field strains of S. Enteritidis with various levels of pathogenicity, providing the basis for future functional characterization of several genes with potential roles in virulence or stress regulation of S. Enteritidis.

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“…Cytochrome bd enhances bacterial tolerance to nitrosative stress [106–111], contributes to mechanisms of detoxification of hydrogen peroxide in E.coli [112–114], suppresses extracellular superoxide production in Enterococcus faecalis [115], and is involved in the degradation of aromatic compounds in Geobacter metallireducens [116]. The A. vinelandii cytochrome bd might be directly involved in energizing Fe-siderophore transport or in reduction of Fe(III)-chelates and, thus, metal liberation in the cytoplasm [117]. As a source of oxidizing power, cytochrome bd -I in E. coli can support disulfide bond formation upon protein folding catalyzed by the DsbA-DsbB system [118], as well as the penultimate step of heme biosynthesis, the conversion of protoporphyrinogen IX into protoporphyrin IX, catalyzed by protoporphyrinogen IX oxidase [119].…”

Section: Physiological Functionsmentioning

confidence: 99%

The cytochrome bd respiratory oxygen reductases

Borisov

Gennis

Hemp

et al. 2011

Biochimica et Biophysica Acta (BBA) - Bioenergetics

448

533

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Summary Cytochrome bd is a respiratory quinol:O2 oxidoreductase found in many prokaryotes, including a number of pathogens. The main bioenergetic function of the enzyme is the production of a proton motive force by the vectorial charge transfer of protons. The sequences of cytochromes bd are not homologous to those of the other respiratory oxygen reductases, i.e., the heme-copper oxygen reductases or alternative oxidases (AOX). Generally, cytochromes bd are noteworthy for their high affinity for O2 and resistance to inhibition by cyanide. In E. coli, for example, cytochrome bd (specifically, cytochrome bd-I) is expressed under O2-limited conditions. Among the members of the bd-family are the so-called cyanide-insensitive quinol oxidases (CIO) which often have a low content of the eponymous heme d but, instead, have heme b in place of heme d in at least a majority of the enzyme population. However, at this point, no sequence motif has been identified to distinguish cytochrome bd (with a stoichiometric complement of heme d) from an enzyme designated as CIO. Members of the bd-family can be subdivided into those which contain either a long or a short hydrophilic connection between transmembrane helices 6 and 7 in subunit I, designated as the Q-loop. However, it is not clear whether there is a functional consequence of this difference. This review summarizes current knowledge on the physiological functions, genetics, structural and catalytic properties of cytochromes bd. Included in this review are descriptions of the intermediates of the catalytic cycle, the proposed site for the reduction of O2, evidence for a proton channel connecting this active site to the bacterial cytoplasm, and the molecular mechanism by which a membrane potential is generated.

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Mutation of cytochromebdquinol oxidase results in reduced stationary phase survival, iron deprivation, metal toxicity and oxidative stress inAzotobacter vinelandii

Cited by 38 publications

References 28 publications

The small protein CydX is required for function of cytochrome bd oxidase in Brucella abortus

The small protein CydX is required for function of cytochrome bd oxidase in Brucella abortus

RNA Sequencing Reveals Differences between the Global Transcriptomes of Salmonella enterica Serovar Enteritidis Strains with High and Low Pathogenicities

The cytochrome bd respiratory oxygen reductases

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