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. 1983 Feb;45(2):600–606. doi: 10.1128/jvi.45.2.600-606.1983

Polyoma virus minichromosomes: poly ADP-ribosylation of associated chromatin proteins.

A Prieto-Soto, B Gourlie, M Miwa, V Pigiet, T Sugimura, N Malik, M Smulson
PMCID: PMC256454  PMID: 6300423

Abstract

The host nuclear enzyme poly(ADP-ribose) polymerase has been shown to be associated with the replicative intermediate and mature forms of polyoma virus minichromosomes. Minichromosome-associated histones H2A and H2B as well as several nonhistone proteins were poly ADP-ribosylated by endogenous poly(ADP-ribose) polymerase. In addition, minichromosome fractions catalyzed the formation in vitro of dimers of endogenous histone H1 linked by poly(ADP-ribose). Poly ADP-ribosylated polyoma virus minichromosome chromatin labeled in vivo with [3H]thymidine could be retained and eluted from anti-poly(ADP-ribose) immunoglobulin G-Sepharose. Pulse-labeled replicative intermediate minichromosomes were retained better on the antibody columns than were mature minichromosomes labeled for 2.5 h. The possible role of poly ADP-ribosylation of viral nucleosomes during polyoma replication or transcription is discussed.

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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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