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PMID: 235125 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

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

Yoshihara K, Tanigawa Y, Burzio L, Koide SS

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
References (21)
21 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1975-01-00
Pages
289-93
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC432289
Subset
IM
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