Literature DB >> 141927

A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele.

F Gibson, G B Cox, J A Downie, J Radik.   

Abstract

A new mutant strain of Escherichia coli in which phosphorylation is uncoupled from electron transport was isolated. The new mutant strain has a similar phenotype to the uncB mutant described previously; results from reconstitution experiments in vitro indicate that the new mutation also affects a component of the F0 portion of the Mg2+-stimulated adenosine triphosphatase. A method was developed to incorporate mutant unc alleles into plasmids. Partial diploid strains were prepared in which the uncB402 allele was incorporated into the plasmid and the new unc mutation into the chromosome, or vice versa. Complementation between the mutant unc alleles was indicated by growth on succinate, growth yields on glucose, ATP-dependent transhydrogenase activities, ATP-induced atebrin-fluorescence quenching and oxidative-phosphorylation measurements. The gene in which the new mutation occurs is therefore distinct from the uncB gene, and the mutant allele was designated uncC424.

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Year:  1977        PMID: 141927      PMCID: PMC1164774          DOI: 10.1042/bj1640193

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  19 in total

1.  Hybridization between Escherichia coli and Shigella.

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2.  Partial diploids of Escherichia coli carrying normal and mutant alleles affecting oxidative phosphorylation.

Authors:  F Gibson; G B Cox; J A Downie; J Radik
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Review 4.  The energetics of bacterial active transport.

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Review 5.  Recalibrated linkage map of Escherichia coli K-12.

Authors:  B J Bachmann; K B Low; A L Taylor
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6.  Isolation and properties of Escherichia coli ATPase mutants with altered divalent metal specificity for ATP hydrolysis.

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Journal:  Biochim Biophys Acta       Date:  1975-10-10

7.  Energy conservation in membranes of mutants of Escherichia coli defective in oxidative phosphorylation.

Authors:  F J Nieuwenhuis; B I Kanner; D L Gutnick; P W Postma; K van Dam
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8.  Oxidative phosphorylation in Escherichia coli K-12: the genetic and biochemical characterisations of a strain carrying a mutation in the uncB gene.

Authors:  J D Butlin; G B Cox; F Gibson
Journal:  Biochim Biophys Acta       Date:  1973-02-22

9.  Differentiation between mutants of Escherichia coli K defective in oxidative phosphorylation.

Authors:  B I Kanner; N Nelson; D L Gutnick
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10.  Oxidative phosphorylation in Escherichia coli K12. An uncoupled mutant with altered membrane structure.

Authors:  G B Cox; F Gibson; L McCann
Journal:  Biochem J       Date:  1974-02       Impact factor: 3.857

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  39 in total

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Authors:  U Norris; P E Karp; A L Fimmel
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2.  A fifth gene (uncE) in the operon concerned with oxidative phosphorylation in Escherichia coli.

Authors:  J A Downie; A E Senior; F Gibson; G B Cox
Journal:  J Bacteriol       Date:  1979-02       Impact factor: 3.490

3.  The uncA gene codes for the alpha-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains.

Authors:  A E Senior; J A Downie; G B Cox; F Gibson; L Langman; D R Fayle
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4.  Properties of membranes from mutant strains of Escherichia coli in which the beta-subunit of the adenosine triphosphatase is abnormal.

Authors:  A E Senior; D R Fayle; J A Downie; F Gibson; G B Cox
Journal:  Biochem J       Date:  1979-04-15       Impact factor: 3.857

5.  Mu-induced polarity in the unc operon of Escherichia coli.

Authors:  F Gibson; J A Downie; G B Cox; J Radik
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6.  Energy transduction in Escherichia coli: new mutation affecting the Fo portion of the ATP synthetase complex.

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Review 7.  Structure and function of H+-ATPase.

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9.  The genes for the eight subunits of the membrane bound ATP synthase of Escherichia coli.

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10.  Redox analysis of the cytochrome o-type quinol oxidase complex of Escherichia coli reveals three redox components.

Authors:  B Bolgiano; I Salmon; W J Ingledew; R K Poole
Journal:  Biochem J       Date:  1991-03-15       Impact factor: 3.857

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