THE BD-TYPE AND BO-TYPE QUINOL OXIDASES HAVE DIFFERENT SUSCEPTIBILITY TO CO

2020 ◽  
Author(s):  
V.B. BORISOV ◽  
◽  
E. FORTE ◽  
S.A. SILETSKY ◽  
M. PETROSINO ◽  
...  
Keyword(s):  
Quinol Oxidases

scholarly journals Respiratory Heterogeneity Shapes Biofilm Formation and Host Colonization in Uropathogenic Escherichia coli

mBio ◽  
2019 ◽  
Vol 10 (2) ◽  
Author(s):  
Connor J. Beebout ◽  
Allison R. Eberly ◽  
Sabrina H. Werby ◽  
Seth A. Reasoner ◽  
John R. Brannon ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Extracellular Matrix ◽  
Bacterial Communities ◽  
Spatial Organization ◽  
Bet Hedging ◽  
Content Type ◽  
Dna Organization ◽  
Quinol Oxidases ◽  
Biofilm Development ◽  
Biofilm Community

ABSTRACT Biofilms are multicellular bacterial communities encased in a self-secreted extracellular matrix comprised of polysaccharides, proteinaceous fibers, and DNA. Organization of these components lends spatial organization to the biofilm community such that biofilm residents can benefit from the production of common goods while being protected from exogenous insults. Spatial organization is driven by the presence of chemical gradients, such as oxygen. Here we show that two quinol oxidases found in Escherichia coli and other bacteria organize along the biofilm oxygen gradient and that this spatially coordinated expression controls architectural integrity. Cytochrome bd, a high-affinity quinol oxidase required for aerobic respiration under hypoxic conditions, is the most abundantly expressed respiratory complex in the biofilm community. Depletion of the cytochrome bd-expressing subpopulation compromises biofilm complexity by reducing the abundance of secreted extracellular matrix as well as increasing cellular sensitivity to exogenous stresses. Interrogation of the distribution of quinol oxidases in the planktonic state revealed that ∼15% of the population expresses cytochrome bd at atmospheric oxygen concentration, and this population dominates during acute urinary tract infection. These data point toward a bet-hedging mechanism in which heterogeneous expression of respiratory complexes ensures respiratory plasticity of E. coli across diverse host niches. IMPORTANCE Biofilms are multicellular bacterial communities encased in a self-secreted extracellular matrix comprised of polysaccharides, proteinaceous fibers, and DNA. Organization of these components lends spatial organization in the biofilm community. Here we demonstrate that oxygen gradients in uropathogenic Escherichia coli (UPEC) biofilms lead to spatially distinct expression programs for quinol oxidases—components of the terminal electron transport chain. Our studies reveal that the cytochrome bd-expressing subpopulation is critical for biofilm development and matrix production. In addition, we show that quinol oxidases are heterogeneously expressed in planktonic populations and that this respiratory heterogeneity provides a fitness advantage during infection. These studies define the contributions of quinol oxidases to biofilm physiology and suggest the presence of respiratory bet-hedging behavior in UPEC.

scholarly journals Antibiotics LL-Z1272 identified as novel inhibitors discriminating bacterial and mitochondrial quinol oxidases

2009 ◽  
Vol 1787 (2) ◽  
pp. 129-133 ◽  
Author(s):  
Tatsushi Mogi ◽  
Hideaki Ui ◽  
Kazuro Shiomi ◽  
Satoshi Ōmura ◽  
Hideto Miyoshi ◽  
...  
Keyword(s):  
Quinol Oxidases

scholarly journals Characterization of thecydAB-Encoded Cytochrome bd Oxidase fromMycobacterium smegmatis

2001 ◽  
Vol 183 (24) ◽  
pp. 7076-7086 ◽  
Author(s):  
Bavesh D. Kana ◽  
Edward A. Weinstein ◽  
David Avarbock ◽  
Stephanie S. Dawes ◽  
Harvey Rubin ◽  
...  
Keyword(s):  
Kanamycin Resistance ◽  
Oxidase Inhibitor ◽  
Growth Defect ◽  
Terminal Oxidase ◽  
Competitive Growth ◽  
Wild Type ◽  
Difference Spectra ◽  
Quinol Oxidases ◽  
Cytochrome Bd Oxidase

ABSTRACT The cydAB genes from Mycobacterium smegmatis have been cloned and characterized. ThecydA and cydB genes encode the two subunits of a cytochrome bd oxidase belonging to the widely distributed family of quinol oxidases found in prokaryotes. ThecydD and cydC genes located immediately downstream of cydB encode a putative ATP-binding cassette-type transporter. At room temperature, reduced minus oxidized difference spectra of membranes purified from wild-type M. smegmatis displayed spectral features that are characteristic of the γ-proteobacterial type cytochrome bd oxidase. Inactivation of cydA or cydB by insertion of a kanamycin resistance marker resulted in loss ofd-heme absorbance at 631 nm. The d-heme could be restored by transformation of the M. smegmatis cyd mutants with a replicating plasmid carrying the highly homologous cydABDC gene cluster fromMycobacterium tuberculosis. Inactivation ofcydA had no effect on the ability of M. smegmatis to exit from stationary phase at 37 or 42°C. The growth rate of the cydA mutant was tested under oxystatic conditions. Although no discernible growth defect was observed under moderately aerobic conditions (9.2 to 37.5 × 102 Pa of pO2 or 5 to 21% air saturation), the mutant displayed a significant growth disadvantage when cocultured with the wild type under extreme microaerophilia (0.8 to 1.7 × 102 Pa of pO2 or 0.5 to 1% air saturation). These observations were in accordance with the two- to threefold increase in cydAB gene expression observed upon reduction of the pO2 of the growth medium from 21 to 0.5% air saturation and with the concomitant increase ind-heme absorbance in spectra of membranes isolated from wild-type M. smegmatis cultured at 1% air saturation. Finally, the cydA mutant displayed a competitive growth disadvantage in the presence of the terminal oxidase inhibitor, cyanide, when cocultured with wild type at 21% air saturation in an oxystat. In conjunction with these findings, our results suggest that cytochrome bd is an important terminal oxidase inM. smegmatis.

Regulation of Cytochromec- and Quinol Oxidases, and Piezotolerance of Their Activities in the Deep-Sea PiezophileShewanella violaceaDSS12 in Response to Growth Conditions

2013 ◽  
Vol 77 (7) ◽  
pp. 1522-1528 ◽  
Author(s):  
Yoshie OHKE ◽  
Ayaka SAKODA ◽  
Chiaki KATO ◽  
Yoshihiro SAMBONGI ◽  
Jun KAWAMOTO ◽  
...  
Keyword(s):  
Deep Sea ◽  
Growth Conditions ◽  
Quinol Oxidases

Functional expression of the Acanthamoeba castellanii alternative oxidase in Escherichia coli; regulation of the activity and evidence for Acaox gene function

2014 ◽  
Vol 92 (3) ◽  
pp. 235-241 ◽  
Author(s):  
Nina Antos-Krzeminska ◽  
Wieslawa Jarmuszkiewicz
Keyword(s):  
Escherichia Coli ◽  
Alternative Oxidase ◽  
Mutual Exclusion ◽  
Acanthamoeba Castellanii ◽  
Functional Expression ◽  
Purine Nucleotides ◽  
E Coli ◽  
Functional Studies ◽  
Product Function ◽  
Quinol Oxidases

To evidence Acanthamoeba castellanii alternative oxidase (AcAOX) gene product function, we studied alterations in the levels of mRNA and protein and AcAOX activity during growth in amoeba batch culture. Moreover, heterologous expression of AcAOX in AOX-deficient Escherichia coli confirmed by the protein immunodetection and functional studies was performed. Despite the presence of native bo and bd quinol oxidases in E. coli membrane, from which the latter is known to be cyanide-resistant, functional expression of AcAOX in E. coli conferred cyanide-resistant benzohydroxamate-sensitive respiration on the bacteria. Moreover, AcAOX activity in transformed bacteria was stimulated by GMP and inhibited by ATP, indicating that AcAOX is regulated by mutual exclusion of purine nucleotides, which was previously demonstrated in the mitochondria of A. castellanii.

scholarly journals Terminal Oxidases of Bacillus subtilisStrain 168: One Quinol Oxidase, Cytochromeaa3 or Cytochrome bd, Is Required for Aerobic Growth

2000 ◽  
Vol 182 (23) ◽  
pp. 6557-6564 ◽  
Author(s):  
Lena Winstedt ◽  
Claes von Wachenfeldt
Keyword(s):  
Bacillus Subtilis ◽  
Sequence Analysis ◽  
Terminal Oxidase ◽  
Rich Medium ◽  
Aerobic Growth ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Cytochrome Bd ◽  
Heme Copper Oxidases ◽  
Quinol Oxidases

ABSTRACT The gram-positive endospore-forming bacterium Bacillus subtilis has, under aerobic conditions, a branched respiratory system comprising one quinol oxidase branch and one cytochrome oxidase branch. The system terminates in one of four alternative terminal oxidases. Cytochrome caa 3 is a cytochromec oxidase, whereas cytochrome bd and cytochromeaa 3 are quinol oxidases. A fourth terminal oxidase, YthAB, is a putative quinol oxidase predicted from DNA sequence analysis. None of the terminal oxidases are, by themselves, essential for growth. However, one quinol oxidase (cytochromeaa 3 or cytochrome bd) is required for aerobic growth of B. subtilis strain 168. Data indicating that cytochrome aa 3 is the major oxidase used by exponentially growing cells in minimal and rich medium are presented. We show that one of the two heme-copper oxidases, cytochrome caa 3 or cytochromeaa 3, is required for efficient sporulation ofB. subtilis strain 168 and that deletion of YthAB in a strain lacking cytochrome aa 3 makes the strain sporulation deficient.

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