Cloning the cyd gene locus coding for the cytochrome d complex of Escherichia coli

Gn, Green; Je, Kranz; Rb, Gennis

doi:10.1016/0378-1119(84)90037-4

Cited by 57 publications

(45 citation statements)

References 20 publications

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“…In E. coli, cydA and cydB encode subunits I and II, respectively, of the cytochrome bd oxidase complex. Subunit I contains cytochrome b558, and subunit II contains cytochromes b595 and d. Mutations in cydB in E. coli result in the loss of spectral features associated with cytochromes b595 and d (12). We show here that A. vinelandii mutants with insertions in the cydB-hybridizing region also lack spectral features associated with cytochromes b595 and d and probably do not synthesize the equivalent of the E. coli cydB gene product (subunit II of the complex).…”

Section: Discussionmentioning

confidence: 70%

“…Plasmid pNG2 contains the structural genes cydA and cydB, encoding subunits I and II of the E. coli cytochrome bd terminal oxidase complex, on a 5.4-kilobase (kb) PvuI-EcoRI fragment cloned in pBR322 (12). pMK1 and pMK2 contain A. vinelandii DNA homologous to the genes cydA and cydB as 8 and 3.6-kb EcoRI fragments, respectively, cloned in pACYC184 (5) (see Results and Fig.…”

Section: Methodsmentioning

confidence: 99%

“…The structural genes cydA and cydB, coding for subunits I and II of the E. coli cytochrome bd terminal oxidase complex, have been cloned (12). In the work presented here, these cloned genes were used as hybridization probes to identify and clone the putative structural genes for the cytochrome bd complex from A. vinelandii.…”

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confidence: 99%

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Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air

et al. 1990

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The genome of Azotobacter vinelandii contains DNA sequences homologous to the structural genes for the Escherichia coli cytochrome bd terminal oxidase complex. Two recombinant clones bearing cydA-and cydB-like sequence were isolated from an A. vinelandii gene library and subcloned into the plasmid vector pACYC184. Physical mapping demonstrated that the cydA-and cydB-like regions in A. vinelandii are contiguous. The cydAB and flanking DNA was mutagenized by the insertion of TnS-B20. Mutations in the cydB-hybridizing region resulted in the loss of spectral features associated with cytochromes b595 and d. A new locus, cydB, encoding cytochromes b595 and d in A. vinelandii is proposed. A second region adjacent to cydB was also involved in expression of the cytochrome bd complex in A. vinelandii, since mutations in this region resulted in an increase in the levels of both cytochrome b595 and cytochrome d. The regions involved in expression of the cytochrome bd complex and cydB are transcribed in the same direction. Mutants deficient in cytochromes b595 and d were unable to grow on N-deficient medium when incubated in air but could fix nitrogen when the environmental 02 concentration was reduced to 1.5% (vol/vol). It is proposed that the branch of the respiratory chain terminated by the cytochrome bd complex supports the high respiration rates required for the respiratory protection of nitrogenase.

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Section: Discussionmentioning

confidence: 70%

Section: Methodsmentioning

confidence: 99%

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Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air

et al. 1990

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“…Two subunits have been described for the cytochrome d complex (21,28). Both subunits are encoded by the cyd operon at 16.5 min on the E. coli chromosome (10,11). It has been suggested that the synthesis of the cytochrome d complex may depend not on the oxygen tension per se but on the ability of the cells to utilize oxygen (35).…”

Section: Discussionmentioning

confidence: 99%

Mutations in the Escherichia coli fnr and tgt genes: control of molybdate reductase activity and the cytochrome d complex by fnr

et al. 1989

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In eubacteria, the tRNA transglycosylase (Tgt) in specific tRNAs exchanges a guanine in the anticodon for 7-aminomethyl-7-deazaguanine, which is finally converted to queuosine. The tgt gene of Escherichia coli has been mapped at 9 min on the genome, and mutant pairs containing an intact or mutated tgt allele were obtained after transduction of the tgt locus by P1 bacteriophages into a genetically defined E. coli strain (S. Noguchi, Y. Nishimura, Y. Hirota, and S. Nishimura, J. Biol. Chem. 257:6544 6550, 1982). These tgt mutants grew anerobicafly with fumarate as an electron acceptor, while nitrate or trimethylamine N-oxide could not be reduced. Furthermore, molybdate reductase activity was almost lacking and the characteristic absorption maxima, corresponding to cytochrome a, and the cytochrome d complex, were not detectable in lowtemperature reduced-minus-oxidized difference spectra in anaerobically grown cells. Transduction of the mutated tgt locus into another E. coli recipient resulted in tgt mutants without anaerobic defects. Transformation of the original tgt mutants with anfnr gene-containing plasmid reversed the anaerobic defects. Clearly, the original tgt mutants harbor a second mutation, affecting the anaerobic regulator protein Fnr. The results suggest that fnr is involved in anaerobic control of components of the cytochrome d complex and of the redox system that transfers electrons to molybdate. F' plasmids containing a fused lacI-lacZ gene with the nonsense codon UAG at different positions in the lacl part were transferred to E. coli strains with a mutated or nonmutated tgt locus but intact infnr. A twofold increase in the frequency of incorrect readthrough of the UAG codon, dependent on the codon context, was observed in the tgt mutant and is suggested to be caused by a tRNATYr with G in place of queuosine.Eseherichia coli mutants with a defined genetic background were isolated, containing or lacking the tRNA guanine transglycosylase (Tgt), and consequently containing or lacking queuosine (Q), 7-(((4,5-cis-dihydroxy-2-cyclopentene-1-yl)-amino)-methyl)-7-deazaguanosine, in tRNA (31).The transglycosylase enzyme catalyzes (in tRNAsGUN specific for Asn, Asp, His, and Tyr) the exchange of the guanine residue in the first position of the anticodon for 7-aminomethyl-7-deazaguanine, a precursor of Q (32, 33). The cyclopentenediol moiety of Q is then synthesized at the level of tRNA and involves epoxy-Q which is finally converted to Q by a cobamide-dependent enzyme system (7).Noguchi et al. (31) isolated tgt mutants by random screening from a collection of Escherichia coli K-12 mutants obtained by treatment with N-methyl-N'-nitrosoguanidine. tRNA was isolated from about 400 strains, and three mutants were found with respective tRNAs containing the anticodon GUN, where N is one of the canonical nucleosides. The defective gene, named tgt, was mapped at about 9 min on the E. coli chromosome, and the gene order was shown to be phoB tgt tsx. The tgt locus was transferred into E. coli ANLO5 (see Table 1) by P1 ba...

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“…There are three heme prosthetic groups associated with this complex comprising cytochromes b558, b595, and d. The two cytochromes b contain protoporphyrin IX (32), and the heme d moiety is a chlorin (44)(45)(46). The genes encoding the subunits of the cytochrome d complex have been cloned and sequenced (16,17). Subunit I is encoded by cydA, and subunit II is encoded by cydB, and these genes are transcribed together in an operon (16).…”

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confidence: 99%

Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli

Oden

Gennis

1991

J Bacteriol

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Cytochrome d terminal oxidase mutants were isolated by using hydroxylamine mutagenesis of pNG2, a pBR322-derived plasmid containing the wild-type cyd operon. The mutagenized plasmid was transformed into a cyo cyd recA strain, and the transformants were screened for the inability to confer aerobic growth on nonfermentable carbon sources. Western blot analysis and visible-light spectroscopy were performed to characterize three independent mutants grown both aerobically and anaerobically. The mutational variants of the cytochrome d complex were stabilized under anaerobic growth conditions. All three mutations perturb the b595 and d heme components of the complex. These mutations were mapped and sequenced and are shown to be located in the N-terminal third of subunit II of the cytochrome d complex. It is proposed that the N terminus of subunit II may interact with subunit I to form an interface that binds the b595 and d heme centers.

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Cloning the cyd gene locus coding for the cytochrome d complex of Escherichia coli

Cited by 57 publications

References 20 publications

Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air

Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air

Mutations in the Escherichia coli fnr and tgt genes: control of molybdate reductase activity and the cytochrome d complex by fnr

Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli

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