Abstract
The molecular basis for the inhibition of the Ca2+,Mg2+-dependent endonuclease resulting from the formation of poly(adenosine diphosphate ribose) (ADP-Rib) was studies in a simplified system containing purified rat liver or bull semen endonuclease, purified rat liver poly(ADP-Rib) synthetase, [3H]NAD+, and DNA. Poly-(adp-rib) synthetase activity was stimulated when Ca2+, Mg2+-dependent endonuclease was added to the reaction mixture in place of histones, suggesting that the endonuclease can act as an acceptor for ADP-Rib. Evidence was presented to show that the ADP-Rib moiety of [3H]NAD+ was incorporated in the endonuclease fraction. The [3H]ADP-Rib bound to the endonuclease was in the form of monomers and oligomers and not long chain polymers. The present results suggest that the Ca2+,Mg2+-dependent endonuclease was ADP-ribosylated when the endonuclease was incubated with poly(ADP-Rib) synthetase and NAD+.
MeSH Terms
Adenosine Diphosphate/metabolism
Animals
Calcium
Cattle
Chromatin/metabolism
Chromatography, Gel
DNA/biosynthesis
Endonucleases/metabolism
Hydrogen-Ion Concentration
Liver/metabolism
Magnesium
Male
NAD/metabolism
Rats
Ribose/metabolism
Semen/metabolism
Tritium
Chemicals
Chromatin
NAD
Tritium
Adenosine Diphosphate
Ribose
DNA
Endonucleases
Magnesium
Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Yoshihara K
Tanigawa Y
Burzio L
Koide S S
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21 references, click to expand
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