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Ribonuclease activity in HeLa cell nuclei is markedly inhibited by ADP-ribosylation following incubation of intact isolated nuclei with [14C]NAD. Time course experiments demonstrate that [14C] incorporation into proteins is accompanied by a 50% inhibition of ribonuclease activity on single-strand and double-strand polynucleotides. Inhibition does not occur when 3-aminobenzamide, a potent (ADP-ribose) polymerase inhibitor, is present. Two enzymatic activities that degrade double-strand polynucleotides have been purified and partially characterized. A relevant level of radioactivity resulting from [14C]NAD incubation of nuclei was associated to the purified enzyme. The RNase F1 component, which shows maximal activity on polyU-polyA is demonstrated to be the major ADP-ribose acceptor protein.
P Quesada, and
M Merola, and
B Farina, and
E Leone
December 1985,
Archives of biochemistry and biophysics,
P Quesada, and
M Merola, and
B Farina, and
E Leone
January 1985,
Biochemical and biophysical research communications,
P Quesada, and
M Merola, and
B Farina, and
E Leone
January 1983,
European journal of biochemistry,
P Quesada, and
M Merola, and
B Farina, and
E Leone
September 1983,
Biochemical and biophysical research communications,
P Quesada, and
M Merola, and
B Farina, and
E Leone
October 1994,
Biochemical and biophysical research communications,
P Quesada, and
M Merola, and
B Farina, and
E Leone
January 1980,
Advances in enzyme regulation,
P Quesada, and
M Merola, and
B Farina, and
E Leone
January 1978,
Methods in cell biology,
P Quesada, and
M Merola, and
B Farina, and
E Leone
January 1978,
Advances in enzyme regulation,
P Quesada, and
M Merola, and
B Farina, and
E Leone
April 1980,
Biochemical Society transactions,
P Quesada, and
M Merola, and
B Farina, and
E Leone
January 1983,
Neurobehavioral toxicology and teratology,
