Assembly of a functional F0 of the proton-translocating ATPase of Escherichia coli

We have investigated both structural and functional assembly of the F0 portion of the Escherichia coli proton-translocating ATPase in vivo. Fractionation of E. coli minicells containing plasmids which code for parts of the unc operon shows that each of the F0 peptides a, b, and c insert into the cyt...

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Bibliographic Details
Published in:The Journal of biological chemistry 1983-08, Vol.258 (16), p.10136-10143
Main Authors: Klionsky, D J, Brusilow, W S, Simoni, R D
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - analysis
Adenosine Triphosphatases - genetics
DNA Restriction Enzymes - metabolism
Electron Transport
Energy Metabolism
Escherichia coli - enzymology
Fluorescence
Macromolecular Substances
Operon
Plasmids
Proton-Translocating ATPases
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Summary:We have investigated both structural and functional assembly of the F0 portion of the Escherichia coli proton-translocating ATPase in vivo. Fractionation of E. coli minicells containing plasmids which code for parts of the unc operon shows that each of the F0 peptides a, b, and c insert into the cytoplasmic membrane independent of each other and without the polypeptides which form the F1 portion of the complex alpha, beta, gamma, delta, and epsilon. Assays of membrane energization indicate that, while formation of a functional proton channel requires the presence of all three F0 polypeptides a, b and c, they are not sufficient. Synthesis of both the alpha and beta subunits of the F1 are required for formation of a functional proton channel.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)44616-3