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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1984-7-2
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pubmed:abstractText |
The activity of purified Ca2+, Mg2+-dependent endonuclease was inhibited when the enzyme was incubated in a system containing poly(ADP-ribose) synthetase, NAD+, Mg2+, and DNA. All four ingredients were essential to mediate ADP-ribosylation and to demonstrate inhibition of the endonuclease. In the absence of Mg2+, ADP-ribose transferring activity of poly(ADP-ribose) synthetase was stimulated by the addition of purified endonuclease to the reaction mixture in a dose-dependent manner. Analysis of the reaction product showed that the endonuclease was ADP-ribosylated. The average chain length of the initial oligo(ADP-ribose) attached to the enzyme was about 5.9 residues. The oligomer was found to be extensively elongated during the chase experiment using unlabeled NAD+ and Mg2+. The present finding suggests that Mg2+ is essential for the extensive elongation of the oligo(ADP-ribose). The DNA-binding affinity of the modified endonuclease was significantly lower than that of unmodified enzyme. Also, free poly(ADP-ribose) was not an effective inhibitor of the endonuclease. These findings suggest that the observed inhibition of the endonuclease induced by ADP-ribosylation is probably due to an electrostatic repulsion between the substrate (DNA) and poly(ADP-ribose) covalently linked to the endonuclease. Histone H1 and H2B stimulated endonuclease activity and were acceptors of ADP-ribose; however, their capacity to stimulate endonuclease activity remained unchanged after ADP-ribosylation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NAD Nucleosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside Diphosphate Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/calcium magnesium dependent...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6579-85
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6327687-Adenosine Diphosphate Ribose,
pubmed-meshheading:6327687-Animals,
pubmed-meshheading:6327687-Cattle,
pubmed-meshheading:6327687-Endodeoxyribonucleases,
pubmed-meshheading:6327687-Kinetics,
pubmed-meshheading:6327687-Male,
pubmed-meshheading:6327687-NAD,
pubmed-meshheading:6327687-NAD+ Nucleosidase,
pubmed-meshheading:6327687-Nucleoside Diphosphate Sugars,
pubmed-meshheading:6327687-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:6327687-Protein Binding,
pubmed-meshheading:6327687-Semen,
pubmed-meshheading:6327687-Tritium
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pubmed:year |
1984
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pubmed:articleTitle |
Mechanism of the inhibition of Ca2+, Mg2+-dependent endonuclease of bull seminal plasma induced by ADP-ribosylation.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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