Two subunits of the F0F1-ATPase are phosphorylated in the inner mitochondrial membrane

Struglics, AndréLund University,Lunds universitet,Ortopedi, Lund,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Orthopaedics (Lund),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine (author)

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.

Fredlund, Kenneth M.Lund University (author)
Møller, Ian M.Lund University (author)
Allen, John F.Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)pcel-jal (author)
Ortopedi, LundSektion III (creator_code:org_t)

In:Biochemical and Biophysical Research Communications: Elsevier BV243:3, s. 664-6680006-291X

By the author/editor: Struglics, André; Fredlund, Kennet ...; Møller, Ian M.; Allen, John F.

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