Kun Ernest, Kirsten Eva, Hakam Alaeddin, Bauer Pal I, Mendeleyev Jerome
Helen Diller Family Comprehensive Cancer Center, Department of Anatomy, University of California-San Francisco, School of Medicine, San Francisco, CA 94143, United States.
FEBS Lett. 2008 Aug 6;582(18):2709-13. doi: 10.1016/j.febslet.2008.06.052. Epub 2008 Jul 9.
The H-bonded complex of ATP with Arg 34 of Zn2+ finger I of poly-ADP-ribose polymerase-1 (PARP-1) determines trans-oligo-ADP-ribosylation from NAD+ to proteins other than PARP-1. This mechanism was tested in lysolecithin fractions of non-malignant and cancer cells separately and after their recombination. Cellular PARP-1 activity was recovered when the centrifugal sediment was recombined with the supernatant fraction containing cellular ADP-ribose oligomer acceptor proteins. Combination of the matrix fraction (Mx) of cancer cells (lacking OXPHOS) with its supernatant had the same PARP-1 activity as the Mx alone. The supernatant of non-malignant cells was replaced by glycolytic enzymes as ADP-ribose acceptor. The hexokinase activity of the supernatant increased when OXPHOS of intact cells was uncoupled by carbonyl cyanide 4-(trifluoro methoxy) phenylhydrazone. trans-ADP-ribosylation was demonstrated by polyacrylamide gel electrophoresis.
