Dependence of trans-ADP-ribosylation and nuclear glycolysis on the Arg 34–ATP complex of Zn 2+ finger I of poly-ADP-ribose polymerase-1

• Published in: FEBS letters Vol. 582; no. 18; pp. 2709 - 2713
• Main Authors: Kun, Ernest, Kirsten, Eva, Hakam, Alaeddin, Bauer, Pal I., Mendeleyev, Jerome
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 06-08-2008
• Subjects: Imidazolyl ADP-ribose; Macromolecular associative control; trans-ADP-ribosylation; LL; Su; HK; trans-ADP-ribosylation; Imidazolyl ADP-ribose; AK; FCCP; Macromolecular associative control; Mx; PARP-1
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2008.06.052

The H-bonded complex of ATP with Arg 34 of Zn
2+ 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.