Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.
- 1 December 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (23) , 7279-7283
- https://doi.org/10.1073/pnas.81.23.7279
Abstract
The ATP synthase complex, designated F1F0, of Escherichia coli is composed of a water-soluble portion (F1; membrane-associated ATPase, EC 3.6.1.3) with ATP-hydrolyzing activity and a membrane-integrated part (F0) with H+-translocating activity. F0 is built up from three kinds of subunits (a, b, and c). We have isolated the F0 portion directly from membranes of an E. coli strain (KY 7485) that overproduces the enzyme several fold. Subunit b was extracted from purified F0 by two methods. One method included prolonged incubation of the F0 complex in the presence of trichloroacetate (2.5 M) and the separation of subunit b and an a-c complex by gel filtration. Alternatively, subunit b was extracted by deoxycholate and separated from the a-c complex by hydrophobic-interaction chromatography. Integrated into liposomes, the a-c complex exhibited neither H+ uptake nor binding of F1. However, a functional F0 complex was reconstituted by adding stoichiometric amounts of subunit b to the a-c complex.This publication has 30 references indexed in Scilit:
- The proton-ATPase of bacteria and mitochondriaThe Journal of Membrane Biology, 1983
- An Asp—Asn substitution in the proteolipid subnit of the ATP‐synthase from Escherichia coli leads to a non‐functional proton channelFEBS Letters, 1982
- E. coli F1-ATPase interacts with a membrane protein component of a proton channelNature, 1982
- ATP‐synthetase complex (F1F0) from Escherichia coliFEBS Letters, 1982
- Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from : Prediction of the primary structure of F0 subunitsBiochemical and Biophysical Research Communications, 1981
- The isolated of F0 of escherichia coli ATP‐synthase is reconstitutively active in H+‐conduction and ATP‐dependent energy‐transductionFEBS Letters, 1981
- Reconstitution of the purified proton conductor (F0) of the adenosine triphosphatase complex from Escherichia coliFEBS Letters, 1980
- Amino acid replacement in dicyclohexylcarbodiimide‐reactive proteins from mutant strains of escherichia coli defective in the energy‐ transducing ATPase complexFEBS Letters, 1980
- Purification of the DCCD‐reactive protein of the energy‐transducing adenosine triphosphatase complex from Escherichia coliFEBS Letters, 1977
- Identification of the DCCD‐reactive protein of the energy transducing adenosinetriphosphatase complex from Escherichia coliFEBS Letters, 1975