Identification of F0 subunits in the rat liver mitochondrial F0F1-ATP synthase

• Published in: Biochimica et biophysica acta Vol. 1058; no. 2; pp. 141 - 146
• Main Authors: Cretin, F, Baggetto, L G, Denoroy, L, Godinot, C
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier 17.06.1991
• Subjects: Adenosine Triphosphatases - isolation & purification; Amino Acid Sequence; Animals; Biochemistry, Molecular Biology; DNA, Mitochondrial - genetics; Electrophoresis, Gel, Two-Dimensional; Life Sciences; Mitochondria, Liver - enzymology; Molecular Sequence Data; Precipitin Tests; Rats
• ISSN: 0006-3002
• DOI: 10.1016/S0005-2728(05)80230-0

In order to identify the subunits constituting the rat liver F0F1-ATP synthase, the complex prepared by selective extraction from the mitochondrial membranes with a detergent followed by purification on a sucrose gradient has been compared to that obtained by immunoprecipitation with an anti-F1 serum. The subunits present in both preparations that are assumed to be authentic components of the complex have been identified. The results show that the total rat liver F0F1-ATP synthase contains at least 13 different proteins, seven of which can be attributed to F0. The following F0 subunits have been identified: the subunit b (migrating as a 24 kDa band in SDS-PAGE), the oligomycin-sensitivity-conferring protein (20 kDa), and F6 (9 kDa) that have N-terminal sequences homologous to the beef-heart ones; the mtDNA encoded subunits 6 (20 kDa) and 8 (less than 7 kDa) that can be synthesized in isolated mitochondria; an additional 20 kDa protein that could be equivalent to the beef heart subunit d.