Two subunits of the FoF1-ATPase are phosphorylated in the inner mitochondrial membrane

André Struglics, Kenneth M. Fredlund*, Ian M. Møller* and John F. Allen§

Plant Cell Biology, Box 7007, Lund University, S-220 07 LUND, Sweden
*Plant Physiology, Lund University, Box 117, S-221 00 Lund, Sweden

§Corresponding author, Phone: +46-46 2227788; Fax: +46-46 2223684; email: john.allen@plantcell.lu.se

Inside-out submitochondrial particles from potato tuber mitochondria were incubated with [g-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 d'-subunit of the F1-ATPase and the b-subunit of the Fo-ATPase, respectively. We suggest that phosphorylation of these proteins may control the interaction between F1 and Fo and regulate energy coupling in oxidative phosphorylation.

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