Identification of poly(ADP-ribose) polymerase-1 as the OXPHOS-generated ATP sensor of nuclei of animal cells

Ernest Kun, Eva Kirsten, Alaeddin Hakam, Pal I. Bauer, Jerome Mendeleyev

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9 Citations (Scopus)


Our results show that in the intact normal animal cell mitochondrial ATP is directly connected to nuclear PARP-1 by way of a specific adenylate kinase enzymatic path. This mechanism is demonstrated in two models: (a) by its inhibition with a specific inhibitor of adenylate kinase, and (b) by disruption of ATP synthesis through uncoupling of OXPHOS. In each instance the de-inhibited PARP-1 is quantitatively determined by enzyme kinetics. The nuclear binding site of PARP-1 is Topo I, and is identified as a critical "switchpoint" indicating the nuclear element that connects OXPHOS with mRNA synthesis in real time. The mitochondrial-nuclear PARP-1 pathway is not operative in cancer cells.

Original languageEnglish
Pages (from-to)568-573
Number of pages6
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - Feb 8 2008



  • Adenylate kinase
  • PARP-1
  • Topo I
  • mRNA

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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