Differential steady-state tyrosine phosphorylation of two oligomeric forms of mitochondrial F0F1ATPsynthase: A structural proteomic analysis

Francesca Di Pancrazio, Elena Bisetto, Vera Alverdi, Irene Mavelli, Gennaro Esposito, Giovanna Lippe

Research output: Contribution to journalArticlepeer-review


We investigated tyrosine phosphorylation of F0F 1ATPsynthase using 3-D blue native (BN)-SDS-PAGE, a refinement of the electrophoretic analysis of mitochondrial complexes. Bovine heart mitochondria were detergent-solubilized and subjected to BN-PAGE. Bands of ATPsynthase monomer (Vmon) and dimer (Vdim) were excised and submitted to SDS-PAGE and immunoblotting. One protein corresponding to F1γ subunit was detected by anti-phosphotyrosine antibody in monomer but not in dimer. This was confirmed by MS peptide mapping. LC-ESI/MS analysis after 3-D SDS-PAGE demonstrated phosphotyrosine in fragment 43-54. NetPhos scores predicted the phosphorylated residue to be Tyr52, in a solvent-accessible loop at the foot of the F1 central stalk.

Original languageEnglish (US)
Pages (from-to)921-926
Number of pages6
Issue number3
StatePublished - Feb 2006


  • Blue native (BN)-PAGE
  • Dimerization
  • Mitochondrial FF ATPsynthase
  • Phosphotyrosines

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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