Identification of poly(ADP-ribose) polymerase-1 as the OXPHOS-generated ATP sensor of nuclei of animal cells.
Biochemical and Biophysical Research Communications(2008)
Abstract
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.
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Key words
Adenylate kinase,PARP-1,OXPHOS,Topo I,mRNA
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