| Autor: |
Guerrieri, Ferruccio, Capozza, Giuseppe, Houštěk, Josef, Zanotti, Franco, Colaianni, Gina, Jirillo, Emilio, Papa, Sergio |
| Zdroj: |
FEBS Letters; June 1989, Vol. 250 Issue: 1 p60-66, 7p |
| Abstrakt: |
The membrane F0, sector of mitochondrial ATP synthase complex was rapidly isolated by direct extraction with CHAPS from F1‐depleted submitochondrial particles. The preparation thus obtained is stable and can be reconstituted in artificial phospholipid membranes to result in oligomycin‐sensitive proton conduction, or recombined with purified F1to give the oligomycin‐sensitive F0F1‐ATPase complex. The F0preparation and constituent polypeptides were characterized by SDS‐polyacrylamide gel electrophoresis and immunoblot analysis. The functional role of F0polypeptides was examined by means of trypsin digestion and reconstitution studies. It is shown that, in addition to the 8 kDa DCCD‐binding protein, the nuclear encoded protein [(1987) J. Mol. Biol. 197, 89–100], characterized as an intrinsic component of F0, (F0I, PVP protein [(1967) J. Biol. Chem. 242, 2547–2551]) is involved in H+translocation and the sensitivity of this process to the F0inhibitors, DCCD and oligomycin. |
| Databáze: |
Supplemental Index |
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