The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide‐insensitive terminal oxidase related to the cytochrome bd quinol oxidases

Cunningham, Louise; Pitt, Melinda; Williams, Huw D.

doi:10.1046/j.1365-2958.1997.3561728.x

Cited by 124 publications

(162 citation statements)

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“…A similar type of oxidase has been described for Pseudomonas nautica 617 (66), P. aeruginosa (67), and Rhodobacter sphaeroides (68).…”

Section: A Novel Oxidase Of Bbј Type In B Subtilis Strain 168 -Thismentioning

confidence: 98%

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A Cytochrome bb′-type Quinol Oxidase inBacillus subtilis Strain 168

Azarkina¹,

Siletsky²,

Borisov³

et al. 1999

Journal of Biological Chemistry

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The aerobic respiratory system of Bacillus subtilis 168 is known to contain three terminal oxidases: cytochrome caa 3 , which is a cytochrome c oxidase, and cytochrome aa 3 and bd, which are quinol oxidases. The presence of a possible fourth oxidase in the bacterium was investigated using a constructed mutant, LUH27, that lacks the aa 3 and caa 3 terminal oxidases and is also deficient in succinate:menaquinone oxidoreductase. The cytochrome bd content of LUH27 can be varied by using different growth conditions. LUH27 membranes virtually devoid of cytochrome bd respired with NADH or exogenous quinol as actively as preparations containing 0.4 nmol of cytochrome bd/mg of protein but were more sensitive to cyanide and aurachin D. The reduced minus oxidized difference spectra of the bd-deficient membranes as well as absorption changes induced by CO and cyanide indicated the presence of a "cytochrome o"-like component; however, the membranes did not contain heme O. The results provide strong evidence for the presence of a terminal oxidase of the bb type in B. subtilis. The enzyme does not pump protons and combines with CO much faster than typical heme-copper oxidases; in these respects, it resembles a cytochrome bd rather than members of the heme-copper oxidase superfamily. The genome sequence of B. subtilis 168 contains gene clusters for four respiratory oxidases. Two of these clusters, cta and qox, are deleted in LUH27. The remaining two, cydAB and ythAB, encode the identified cytochrome bd and a putative second cytochrome bd, respectively. Deletion of ythAB in strain LUH27 or the presence of the yth genes on plasmid did not affect the expression of the bb oxidase. It is concluded that the novel bb-type oxidase probably is cytochrome bd encoded by the cyd locus but with heme D being substituted by high spin heme B at the oxygen reactive site, i.e. cytochrome b 558 b 595 b.

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“…A similar type of oxidase has been described for Pseudomonas nautica 617 (66), P. aeruginosa (67), and Rhodobacter sphaeroides (68).…”

Section: A Novel Oxidase Of Bbј Type In B Subtilis Strain 168 -Thismentioning

confidence: 98%

“…In addition, the new oxidase binds CO much faster than is typical of heme-copper oxidases, although still slower than the bd-type oxidase in the same strain. It is notable that P. aeruginosa contains a terminal oxidase of the bd type seemingly operating in the absence of heme D (67).…”

Section: A Novel Oxidase Of Bbј Type In B Subtilis Strain 168 -Thismentioning

confidence: 99%

A Cytochrome bb′-type Quinol Oxidase inBacillus subtilis Strain 168

Azarkina¹,

Siletsky²,

Borisov³

et al. 1999

Journal of Biological Chemistry

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“…Both inhibitors also reduced degradation of the respective substrates to the same extent as they inhibited respiration (not shown). To account for the influence of cyanide-insensitive respiration (Cunningham et al 1997), we investigated a cioB mutant which is defective in the cyanide-insensitive cytochrome c oxidase Cio (Cooper et al 2003). KCN inhibited the substrate-dependent oxygen uptake in this mutant completely (Table 1).…”

Section: Characterization Of Cells From Aggregatesmentioning

confidence: 99%

Cell aggregation of Pseudomonas aeruginosa strain PAO1 as an energy-dependent stress response during growth with sodium dodecyl sulfate

et al. 2006

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Pseudomonas aeruginosa strain PAO1 grew with the detergent sodium dodecyl sulfate (SDS). The growth started with the formation of macroscopic cell aggregates which consisted of respiring cells embedded in an extracellular matrix composed of acidic polysaccharides and DNA. Damaged and uncultivable cells accumulated in these aggregates compared to those cells that remained suspended. We investigated the response of suspended cells to SDS under different conditions. At high energy supply, the cells responded with a decrease in optical density and in viable counts, release of protein and DNA, and formation of macroscopic aggregates. This response was not observed if the energy supply was reduced by inhibiting respiration with KCN, or if cells not induced for SDS degradation were exposed to SDS. Exposure to SDS caused cell lysis without aggregation if cells were completely deprived of energy, either by applying anoxic conditions, by addition of CCCP, or by addition of KCN to a mutant defective in cyanideinsensitive respiration. Aggregated cells showed a more than 100-fold higher survival rate after exposure to SDS plus CCCP than suspended cells. Our results demonstrate that cell aggregation is an energy-dependent response of P. aeruginosa to detergent stress which might serve as a survival strategy during growth with SDS.

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“…1). The exception is the cyanide-insensitive oxidase (CIO), encoded by the cioAB operon, which is homologous to the cytochrome bd quinol oxidases of Escherichia coli and Azotobacter vinelandii (Cunningham & Williams, 1995;Cunningham et al, 1997;Junemann, 1997), and as such shows no homology to members of the ubiquitous haem-copper oxidase superfamily (Garcia-Horsman et al, 1994). CioA and CioB are homologous to the two subunits of the cytochrome bd quinol oxidase, CydA and CydB, of E. coli.…”

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confidence: 99%

Regulation of expression of the cyanide-insensitive terminal oxidase in Pseudomonas aeruginosa

2003

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The regulation of the cyanide-insensitive oxidase (CIO) in Pseudomonas aeruginosa, a bacterium that can synthesize HCN, is reported. The expression of a cioA-lacZ transcriptional fusion, CioA protein levels and CIO activity were low in exponential phase but induced about fivefold upon entry into stationary phase. Varying the O 2 transfer coefficient from 11?5 h 21 to 87?4 h 21 had no effect on CIO expression and no correlation was observed between CIO induction and the dissolved O 2 levels in the growth medium. However, a mutant deleted for the O 2 -sensitive transcriptional regulator ANR derepressed CIO expression in an O 2 -sensitive manner, with the highest induction occurring under low-O 2 conditions. Therefore, CIO expression can respond to a signal generated by low O 2 levels, but this response is normally kept in check by ANR repression. ANR may play an important role in preventing overexpression of the CIO in relation to other terminal oxidases. A component present in spent culture medium was able to induce CIO expression. However, experiments with purified N-butanoyl-L-homoserine lactone or N-(3-oxododecanoyl)homoserine lactone ruled out a role for these quorum-sensing molecules in the control of CIO expression. Cyanide was a potent inducer of the CIO at physiologically relevant concentrations and experiments using spent culture medium from a DhcnB mutant, which is unable to synthesize cyanide, showed that cyanide was the inducing factor present in P. aeruginosa spent culture medium. However, the finding that in a DhcnB mutant cioA-lacZ expression was induced normally upon entry into stationary phase indicated that cyanide was not the endogenous inducer of the terminal oxidase. The authors suggest that the failure of O 2 to have an effect on CIO expression in the wild-type can be explained either by the requirement for an additional, stationary-phase-specific inducing signal or by the loss of an exponential-phase-specific repressing signal. INTRODUCTIONPseudomonas aeruginosa is an opportunistic pathogen that causes a variety of nosocomial infections, including pneumonia, urinary tract infections, surgical wound infections, and bloodstream infections (for a review see Deretic, 2000). It causes life-threatening illness in patients with cystic fibrosis. Initially, P. aeruginosa colonizes the airways with other pathogens such as Haemophilus influenzae and Staphylococcus aureus. However, in most of these patients chronic lung disease develops in which the bacterial population consists almost exclusively of P. aeruginosa in the form of biofilms (Govan & Deretic, 1996). P. aeruginosa is a facultative anaerobe that preferentially obtains its energy via aerobic respiration, but it is well adapted to conditions of limited O 2 supply (Palleroni, 1984;Davies et al., 1989). It is capable of anaerobic growth with nitrate as a terminal electron acceptor and in the absence of nitrate it is able to ferment arginine, generating ATP by substrate-level phosphorylation (Palleroni, 1984;Davies et al., 1989;Van der Wauven et ...

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The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide‐insensitive terminal oxidase related to the cytochrome bd quinol oxidases

Cited by 124 publications

References 55 publications

A Cytochrome bb′-type Quinol Oxidase inBacillus subtilis Strain 168

A Cytochrome bb′-type Quinol Oxidase inBacillus subtilis Strain 168

Cell aggregation of Pseudomonas aeruginosa strain PAO1 as an energy-dependent stress response during growth with sodium dodecyl sulfate

Regulation of expression of the cyanide-insensitive terminal oxidase in Pseudomonas aeruginosa

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