Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F sub(1)F sub(o)-ATPase alter the coupling of F sub(1) to F sub(o)

The conserved Pro super(43) residue of the uncE protein (subunit c) of the Escherichia coli F sub(1)F sub(o)-ATPase was changed to Ser or Ala by oligonucleotide-directed mutagenesis, and the mutations were incorporated into the chromosome. The resultant mutant strains were capable of oxidative phosp...

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Bibliographic Details
Published in:The Journal of biological chemistry 1989-01, Vol.264 (1), p.305-311
Main Authors: Miller, MJ, Fraga, D, Paule, C R, Fillingame, R H
Format: Article
Language:English
Subjects:
Escherichia coli
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Summary:The conserved Pro super(43) residue of the uncE protein (subunit c) of the Escherichia coli F sub(1)F sub(o)-ATPase was changed to Ser or Ala by oligonucleotide-directed mutagenesis, and the mutations were incorporated into the chromosome. The resultant mutant strains were capable of oxidative phosphorylation. The results support the idea that Pro super(43), and neighboring conserved polar residues play an important role in the binding and functional coupling of F sub(1) to F sub(o). Although a Pro residue is found at position 43 in all species of subunit c studied, surprisingly, it is not absolutely essential to function.
ISSN:0021-9258