Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA

Oden, Kristine L.; DeVeaux, Linda C.; Vibat, Cecile Rose T.; Cronan, John E.; Gennis, Robert B.

doi:10.1016/0378-1119(90)90337-q

Cited by 91 publications

(54 citation statements)

References 40 publications

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“…(27). Kanr Aps colonies were isolated, which presumably have recombined the Kanr marker into the sohB gene on the chromosome with subsequent loss of the Apr plasmid.…”

Section: Resultsmentioning

confidence: 99%

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Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype

et al. 1991

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We cloned and sequenced the sohB gene of Escherichia coli. The temperature-sensitive phenotype of bacteria that carry a Tn10 insertion in the htrA (degP) gene is relieved when the sohB gene is present in the cell on a multicopy plasmid (30 to 50 copies per cell). The htrA gene encodes a periplasmic protease required for bacterial viability only at high temperature, i.e., above 39 degrees C. The sohB gene maps to 28 min on the E. coli chromosome, precisely between the topA and btuR genes. The gene encodes a 39,000-Mr precursor protein which is processed to a 37,000-Mr mature form. Sequencing of a DNA fragment containing the gene revealed an open reading frame which could encode a protein of Mr 39,474 with a predicted signal sequence cleavage site between amino acids 22 and 23. Cleavage at this site would reduce the size of the processed protein to 37,474 Mr. The predicted protein encoded by the open reading frame has homology with the inner membrane enzyme protease IV of E. coli, which digests cleaved signal peptides. Therefore, it is possible that the sohB gene encodes a previously undiscovered periplasmic protease in E. coli that, when overexpressed, can partially compensate for the missing HtrA protein function.

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“…(27). Kanr Aps colonies were isolated, which presumably have recombined the Kanr marker into the sohB gene on the chromosome with subsequent loss of the Apr plasmid.…”

Section: Resultsmentioning

confidence: 99%

“…The method of Oden et al (27) Nucleotide sequence accession number. This sequence has been given the GenBank accession number M73320.…”

Section: Methodsmentioning

confidence: 99%

Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype

et al. 1991

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“…Cytochrome bo-type quinol oxidase was purified from the cytochrome bd-deficient strain GO103 (Acyd:: Km' [25]) harboring pHN3795-I (H. Nakamura, unpublished results), as described previously [8]. pHN3795-I is a derivative of pBR322 which carries the cytochrome bo operon (cyoABCDG) and was obtained from pHN3795 [26] as a clone that can support the aerobic growth of the dcyo Acyd strain on a nonfermentable carbon source.…”

Section: Methodsmentioning

confidence: 99%

Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

et al. 1994

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Reaction intermediates in dioxygen reduction by the E. coli cytochrome bo-type ubiquinol oxidase were studied by time-resolved resonance Raman spectroscopy using the artificial cardiovascular system. At O-20 ps following photolysis of the enzyme-CO adduct in the presence of 0,, we observed the Fe&& stretching Raman band at 568 cm-' which shifted to 535 cm-' with the "0, derivative. These frequencies are remarkably close to those of other oxyhemoproteins including dioxygen-bound hemoglobin and aa,-type cytochrome c oxidase. In the later time range (20-40 ps), other oxygen-isotope-sensitive Raman bands were observed at 788 and 361 cm-'. Since the 781 cm-' band exhibited a downshift by 37 cm-' upon '*O, substitution, we assigned it to the Fe'"=0 stretching mode. This band is considered to arise from the ferry1 intermediate, but its appearance was much earlier than the corresponding intermediate of bovine cytochrome c oxidase (>I00 ps). The 361 cn-' band showed the '60/'s0 isotopic frequency shift of I4 cm-' similar to the case of bovine cytochrome c oxidase reaction.

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“…cyd mutants are unable to grow aerobically on nonfermentable carbon sources in the presence of trace amounts of zinc (ZAB plates), a potent inhibitor of components of the respiratory electron transfer system, especially cytochrome o (32). A strain harboring the cydB::mini-TnlO allele did not grow on ZAB plates, while the parental strain B178 did ( [30]) or the Acyd::Camr deletion/substitution (complete deletion of the cyd operon [20]) was transduced into either B178 or GR70N (30), all of the resulting transductants were Ts-at 37°C and exhibited all other phenotypes associated with our cydB::mini-TnlO mutation (Fig. 2Bb).…”

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confidence: 99%

arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon

et al. 1992

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DNA sequencing analyses showed that the mini-TnlO insertion resides in the cydB gene, the distal gene of the cydAB operon (cytochrome d). The Ts-growth phenotype was also shown to be associated with previously described cyd alleles. In addition, all cyd mutants were found to be extremely sensitive to hydrogen peroxide.Northern (RNA) blot analysis showed that cyd-specific mRNA levels accumulate following a shift to high temperature. Interestingly, this heat shock induction of the cyd operon was not affected in an rpoHA background but was totally absent in an arcA or arcB mutant background. Extragenic suppressors of the Cyd Ts-phenotype are found at _10-3. Two extragenic suppressors were shown to be null alleles in either arcA or arcB. One interpretation of our results is that in the absence of ArcA or ArcB, which are required for the repression of the cyo operon (cytochrome o), elevated levels of Cyo are produced, thus compensating for the missing cytochrome d function. Consistent with this interpretation, the presence of the cyo gene on a multicopy

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Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA

Cited by 91 publications

References 40 publications

Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype

Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype

Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon

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Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA

Cited by 91 publications

References 40 publications

Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype

Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype

Observation of the Fe–O2 and FeIV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon

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Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli