Two subunits of the F0F1-ATPase are phosphorylated in the inner mitochondrial membrane
Forskningsoutput: Tidskriftsbidrag › Artikel i vetenskaplig tidskrift
Inside-out submitochondrial particles from potato tuber mitochondria were incubated with [γ-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 δ'-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.
|Enheter & grupper|
|Tidskrift||Biochemical and Biophysical Research Communications|
|Status||Published - 1998 feb 24|
|Peer review utförd||Ja|