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PMID: 141927 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 164 ·No. 1 ·1977-04-15 ·Pages 193-8

Gibson F, Cox GB, Downie JA, Radik J

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.

MeSH Terms
Adenosine Triphosphatases/metabolism Alleles Diploidy Electron Transport Escherichia coli/enzymology Genes Models, Biological Mutation Oxidative Phosphorylation
Chemicals
Adenosine Triphosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Gibson F
Cox G B
Downie J A
Radik J
References (19)
19 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1977-04-15
Pages
193-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1164774
Subset
IM
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