Orientation of chargerin II (A6L) in the ATP synthase of rat liver mitochondria determined with antibodies against peptides of the protein.
Previous studies suggested that the hydrophobic protein chargerin II, which is encoded in the unidentified reading frame A6L of mitochondrial DNA (URFA6L), may have a key role in the energy transduction by mitochondrial ATP synthase because an antibody against chargerin II inhibited ATP synthesis and ATP-Pi exchange, in an energy-dependent fashion. In the present work, the orientation of chargerin II in Fo of the ATP synthase of rat liver mitochondria was examined using antibodies against peptides of chargerin II. Results showed that its N-terminal region (about 8 amino acid residues) was exposed on the surface of the C-side of Fo, but its C-terminal and charge-cluster regions were buried in Fo.
Oda
T
T
Faculty of Pharmaceutical Sciences, University of Tokushima, Japan.
Futaki
S
S
Kitagawa
K
K
Yoshihara
Y
Y
Tani
I
I
Higuti
T
T
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex / Q000032:analysis; D015151:Immunoblotting; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D051381:Rats; D013367:Submitochondrial Particles / Q000201:enzymology
D000906:Antibodies; D000936:Antigen-Antibody Complex; D008565:Membrane Proteins; C044593:chargerins; D006180:Proton-Translocating ATPases