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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 Aug;71(8):3212–3216. doi: 10.1073/pnas.71.8.3212

Poly(ADP-Ribose): Release of Template Restriction in HeLa Cells

Jerry H Roberts 1, Patricia Stark 1, Mark Smulson 1
PMCID: PMC388653  PMID: 4370271

Abstract

Evidence is presented to show that ADP-ribosylation of nuclear proteins by poly(ADP-ribose) polymerase enhances template-primer activity of HeLa cell nuclear DNA. We used Escherichia coli DNA polymerase I (EC 2.7.7.7; DNA nucleotidyltransferase) as an exogenous probe of nuclear DNA status. Neither NAD nor free poly(ADP-ribose) acts directly on the bacterial enzyme. The stimulation is specific for formation of ADP-ribosylated proteins and is not a generalized polyanion or nucleotide effect on chromatin. The release of template restriction is proportional to the capacity of a given cell line to synthesize poly(ADP-ribose); both the stimulation and poly(ADP-ribose) formation are coordinately proportional to NAD concentration. Binding studies with DNA polymerase indicate exposure or generation of additional 3′-OH primer sites due to ADP-ribosylation in intact nuclei. With intact cells, there appears a correlation among growth, physiological template restriction, and the above effects of ADP-ribosylation.

Keywords: NAD, nuclear proteins, DNA polymerase, DNA primer sites

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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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