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. 1975 Jan;72(1):289–293. doi: 10.1073/pnas.72.1.289

Evidence for adenosine diphosphate ribosylation of Ca2+, Mg2+-dependent endonuclease.

K Yoshihara, Y Tanigawa, L Burzio, S S Koide
PMCID: PMC432289  PMID: 235125

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+.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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