THE EFFECTS OF AN ATPE RIBOSOME-BINDING SITE MUTATION ON THE STOICHIOMETRY OF THE C-SUBUNIT IN THE F1F0 ATPASE OF ESCHERICHIA-COLI

Autor(en): SCHEMIDT, RA
HSU, DKW
DECKERSHEBESTREIT, G
ALTENDORF, K 
BRUSILOW, WSA
Stichwörter: Biochemistry & Molecular Biology; Biophysics; CHANNEL; DICYCLOHEXYLCARBODIIMIDE; F0 COMPLEX; GENES; H+-ATPASE; OPERON; PROTEIN; PROTON-TRANSLOCATING ATPASE; UNC
Erscheinungsdatum: 1995
Herausgeber: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS
Enthalten in: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Band: 323
Ausgabe: 2
Startseite: 423
Seitenende: 428
Zusammenfassung: 
We tested the hypothesis that the stoichiometry of the c subunit in the F-0 sector of the Escherichia coli F1F0 ATPase is dependent upon the level of atpE gene expression. F-0 was purified from cells carrying plasmids encoding the F-0 subunits with and without a ribosome-binding site mutation preceding atpE, the gene which codes for the c subunit. Subunit-specific antibodies were used to quantitate the relative amounts of the b and c subunits. The decreased expression of atpE resulted in a significantly decreased amount of the c subunit in the purified F-0. Immunoblot quantitation of the amounts of b and c subunits in F1F0 precipitated by anti-F-1 antiserum also showed that the mutation produced significant differences in the stoichiometry of subunit c. The amount of c subunit assembled into the F1F0 synthesized from a plasmid carrying the atpE ribosome binding site mutation was 2-5 times less than the amount found in the F1F0 synthesized from a wild-type plasmid, Therefore, the stoichiometry of the c subunit assembled into the F1F0 complex appears to be variable, depending on the expression of atpE. (C) 1995 Academic Press, Inc.
ISSN: 00039861
DOI: 10.1006/abbi.1995.0063

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