Catalytic inhibition of DNA topoisomerase IIalpha by sodium azide

Toxicology Letters
R JuR D Snyder

Abstract

It has been demonstrated previously that sodium azide reduces the clastogenicity of several DNA topoisomerase II (topo II) poisons in cultured mammalian cells. These studies suggested that azide may be a catalytic topo II inhibitor. Azide interferes with mitochondrial production of ATP and is also known to inhibit cellular ATPases. Since topo II requires ATP for catalytic activity (enzyme turnover), it seemed likely that interference with ATP levels or ATP catabolism was the underlying mechanism of topo II inactivation; however, this has not been examined in living cells under conditions where the endogenous topo II is active on genomic DNA. The present studies were carried out to verify that azide inhibits endogenous topo II in cells. We show that azide blocks both decatenation and relaxation activity of purified topo II in a concentration dependent manner and reduces topoII/DNA covalent complex formation in cells. From these studies, it is concluded that sodium azide catalytically inactivates topo II via an ATP-sensitive process.

References

Jan 11, 1990·Nucleic Acids Research·J R SpitznerM T Muller
Jan 1, 1994·Advances in Pharmacology·A H AndersenO Westergaard
Jan 1, 1996·Annual Review of Biochemistry·J C Wang
Sep 3, 1998·The Journal of Biological Chemistry·E Vasilyeva, M Forgac
Oct 16, 1999·Proceedings of the National Academy of Sciences of the United States of America·H GaoR M Snapka

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Citations

May 27, 2006·Proceedings of the National Academy of Sciences of the United States of America·Matthew W BowlerJohn E Walker
Nov 26, 2004·The Journal of Parasitology·Dietmar Steverding, Stefan Scory
May 10, 2019·Communications Biology·Tina S Skinner-AdamsKatherine T Andrews
Jan 12, 2020·Communications Biology·Tina S Skinner-AdamsKatherine T Andrews

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