Identification of subunit I as the cytochrome b558 component of the cytochrome d terminal oxidase complex of Escherichia coli.

Green, G. N.; Kranz, Robert G.; Lorence, Robert M.; Gennis, Robert B.

doi:10.1016/s0021-9258(17)42891-2

Cited by 67 publications

(9 citation statements)

References 18 publications

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“…The cydA and cydB encode subunits of the cytochrome bd terminal oxidase [ 49 ] and act as an electron-transfer complex in oxidative phosphorylation. The complex has high NO dissociation rate and notable catalase activity and is required for Salmonella to defend against nitrosative or peroxidative stress [ 50 ].…”

Section: Discussionmentioning

confidence: 99%

Gene essentiality profiling reveals a novel determinant of stresses preventing protein aggregation in Salmonella

Wang

Zhu

et al. 2022

Emerging Microbes & Infections

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Adaptation to various stresses during infection is important for Salmonella Typhimurium virulence, while the fitness determinants under infection-relevant stress conditions remain unknown. Here, we simulated conditions Salmonella encountered within the host or in the environment by 15 individual stresses as well as two model cell lines (epithelium and macrophage) to decipher the genes and pathways required for fitness. By high-resolution Tn-seq analysis, a total of 1242 genes were identified as essential for fitness under at least one stress condition. The comparative analysis of fitness determinants in 17 stress conditions indicated the essentiality of genes varied in different mimicking host niches. A total of 12 genes were identified as fitness determinants in all stress conditions, including recB , recC , and xseA (encode three exonuclease subunits necessary for DNA recombination repair) and a novel essential fitness gene yheM . YheM is a putative sulfurtransferase subunit that is responsible for tRNA modification, and our results showed that Salmonella lacking yheM accumulated more aggregates of endogenous protein than wild-type. Moreover, we established a scoring scheme for sRNA essentiality analysis and found STnc2080 of unknown function was essential for resistance to LL-37. In summary, we systematically dissected Salmonella gene essentiality profiling and demonstrated the general and specific adaptive requirements in infection-relevant niches. Our data not only provide valuable insights on how Salmonella responds to environmental stresses during infections but also highlight the potential clinical application of fitness determinants in vaccine development.

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Section: Discussionmentioning

confidence: 99%

Gene essentiality profiling reveals a novel determinant of stresses preventing protein aggregation in Salmonella

Wang

Zhu

et al. 2022

Emerging Microbes & Infections

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“…Sodium (V-lauroylsarcosine and Zwittergent 3-12 denatured cytochrome 6558. Zwittergent is used to solubilize the cytochrome d complex (Miller & Gennis, 1983), yet it denatures cytochrome 6558 from strain GR84N[pNGlO], Apparently, subunit II of the complex, which is missing from this strain, protects subunit I from denaturation as it also protects subunit I from limited proteolysis (Green et al, 1984b). The extent of denaturation of cytochrome 6558 was monitored spectroscopically after each of the two DEAE column chromatography steps of the purification.…”

Section: Discussionmentioning

confidence: 99%

“…Cytochrome bS9S has a second absorbance peak at 560 nm that overlaps with the absorbance of cytochrome b}SS (Koland et al, 1984), an overlap that has made the quantitation of cytochrome bs58 difficult. Subunit I has been previously shown (Green et al, 1984b) to be the cytochrome b55i component 0006-2960/86/0425-2309501.50/0 © 1986 American Chemical Society of the complex, but attempts to separate the two subunits of the purified complex have resulted in denaturation and loss of heme (M. Miller, personal communication). In this report, an alternative method was used to obtain purified cytochrome 6558 from a strain overproducing this protein.…”

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confidence: 99%

“…Strain and Growth Condition. E. coli strain GR84N-[pNGlO], cydAl, nadAl, rpsL, recA, was grown at 150 rpm in a 250-L fermentor at a sparge rate of 2 ft3/min in a sodium DL-lactate minimal medium supplemented with nicotinic acid, casamino acids, and tetracycline (Tet)1 * (Green et al, 1984b). The antibiotic helps to maintain the plasmid pNGlO.…”

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confidence: 99%

“…The antibiotic helps to maintain the plasmid pNGlO. E. coli strains containing cyd A mutations do not contain either subunit of the cytochrome d complex (Green et al, 1984b).…”

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confidence: 99%

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Specific overproduction and purification of the cytochrome b558 component of the cytochrome d complex from Escherichia coli

Green¹,

Lorence²,

Gennis³

1986

Biochemistry

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In Escherichia coli strain GR84N[pNG10], the cloned gene for subunit I of the membrane-bound cytochrome d complex resulted in the overproduction of cytochrome b558 and facilitated purification of this cytochrome. Extracting membranes with 1% Triton X-100 followed by two chromatographic steps yielded a single band on sodium dodecyl sulfate-polyacrylamide gels corresponding to subunit I (Mr 57 000). Purified cytochrome b558 was in its native state as determined by difference absorption spectroscopy and by potentiometric analysis. Both the membranes of strain GR84N[pNG10] and the purified subunit I lacked the other two spectroscopically defined cytochromes, b595 (previously "a1") and d, of the cytochrome d complex. Reconstitution of cytochrome b558 in phospholipid vesicles demonstrated that cytochrome b558 can be reduced by ubiquinol but that it does not reduce molecular oxygen. Heme extraction of cytochrome b558 yielded an extinction coefficient of 22 000 M-1 cm-1 for the wavelength pair of 560 and 580 nm in the reduced-minus-oxidized spectrum. The mutation on pNG10 that eliminates subunit II was mapped to a 250 base pair DNA fragment.

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Resonance raman study on axial ligands of heme irons in cytochrome bd‐type ubiquinol oxidase from Escherichia coli

Hirota¹,

Mogi²,

Anraku³

et al. 1995

Biospectroscopy

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SYNOPSISResonance Raman ( R R ) spectra of cytochrome bd-type ubiquinol oxidase enriched with Fe-isotopes were investigated with excitation at 406.7,424.0,427.0, 441.6, and 647.1 nm. The hands of reduced form a t 252 and 400 cm-' were tentatively assigned to u p e -~i s of high-spin bSg5 and vFePMet of low-spin respectively. The uFe-O, and 6FeO0 bands of heme d-O2 were observed at 566 and -445 cm-', respectively. The vpe-cO frequency of heme d -CO was unusually low (477 cm-') but the u4 frequency was not of P-450 type. Therefore, the axial ligand of heme d would not be an ordinary histidine or cysteine. 0 1995 John

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Identification of subunit I as the cytochrome b558 component of the cytochrome d terminal oxidase complex of Escherichia coli.

Cited by 67 publications

References 18 publications

Gene essentiality profiling reveals a novel determinant of stresses preventing protein aggregation in Salmonella

Gene essentiality profiling reveals a novel determinant of stresses preventing protein aggregation in Salmonella

Specific overproduction and purification of the cytochrome b558 component of the cytochrome d complex from Escherichia coli

Resonance raman study on axial ligands of heme irons in cytochrome bd‐type ubiquinol oxidase from Escherichia coli

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