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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kun E,Kirsten E,Hakam A,Bauer PI,Mendeleyev J

doi

10.1016/j.bbrc.2007.12.004

subject

Has Abstract

pub_date

2008-02-08 00:00:00

pages

568-73

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)02622-8

journal_volume

366

pub_type

杂志文章

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