Two subunits of the F0F1-ATPase are phosphorylated in the inner mitochondrial membrane.
Inside-out submitochondrial particles from potato tuber mitochondria were incubated with [gamma-32P]ATP. More than 16 phosphorylated polypeptides were detected by autoradiography on an SDS-gel. Two phosphoproteins, migrating at 22 and 28 kDa, were excised from the SDS-gel, electroeluted, and purified further by anion chromatography. The phosphoproteins were N-terminally sequenced. Over the regions sequenced, the 22 and 28 kDa phosphoproteins had 100% sequence identity with potato proteins identified as the delta'-subunit of the F1-ATPase and the b-subunit of the F0-ATPase, respectively. We suggest that phosphorylation of these proteins may control the interaction between F1 and F0 and regulate energy coupling in oxidative phosphorylation.
Struglics
A
A
Plant Cell Biology, Lund University, Sweden.
Fredlund
K M
KM
Møller
I M
IM
Allen
J F
JF
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D001345:Autoradiography; D004591:Electrophoresis, Polyacrylamide Gel; D007425:Intracellular Membranes / Q000201:enzymology*; D008928:Mitochondria / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010750:Phosphoproteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D017421:Sequence Analysis; D011198:Solanum tuberosum / Q000648:ultrastructure*; D013045:Species Specificity
D010750:Phosphoproteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases