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Plant and Cell Physiology, 1999, Vol. 40, No. 12 1271-1279
© 1999

Phosphoproteins and Protein Kinase Activities Intrinsic to Inner Membranes of Potato Tuber Mitochondria

André Struglics1, Kenneth M. Fredlund2,3, Ian M. Møller2 and John F. Allen1,4

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

3 Corresponding author: E-mail, john.allen{at}plantcell.lu.se; Fax, +46-46-2223684

Inside-out submitochondrial particles (IO-SMP) were isolated and purified from potato (Solanum tuberosum L. cv.) tubers. When these IO-SMP were incubated with [{gamma} 32P]ATP more then 20 proteins became labelled as a result of phosphorylation. The 32P incorporation was stimulated by the oxidising reagent ferricyanide. Except for a 17 kDa protein which was phosphorylated only in the absence of divalent cations, the protein phosphorylation required Mg2+. The time for half-maximum 32P incorporation was 4 mm for the 22 kDa phospho-F1 {delta}-subunit and 2 min for the 28 kDa phospho-F0 b-subunit of the proton-ATPase. The Km for ATP for the detected phosphoproteins was between 65 µM and 110 µM. The pH optimum for protein phosphorylation in inner membranes was between pH 6 and 8, and for the F1 {delta}-subunit and the F0 b-subunit the pH optima were 6.5–8 and pH 8, respectively. A 37 kDa phosphoprotein was phosphorylated on a histidine residue while the remainder of the inner membrane proteins were phosphorylated on serine or threonine residues. Two autophosphorylated putative kinases were identified: one at 16.5 kDa required divalent cations for autophosphorylation, while another at 30 kDa did not. A 110 kDa protein was labelled only with [{alpha}-32P] suggesting adenylylation.

3 Present address; Novartis Seeds AB, Box 302, S-261 23 Landskrona, Sweden.

(Received July 5, 1999; Accepted October 13, 1999)
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