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. 1981 May;38(2):548–555. doi: 10.1128/jvi.38.2.548-555.1981

Virus-coded DNA endonuclease from avian retrovirus.

M Golomb, D P Grandgenett, W Mason
PMCID: PMC171185  PMID: 6165835

Abstract

Reverse transcriptase from avian retrovirus has a physically associated DNA endonuclease with novel substrate and cofactor requirements. A similar endonuclease activity copurifies with pp32, a protein from viral cores that has been identified with the non-alpha region of the beta subunit of reverse transcriptase. Several temperature-sensitive mutants of avian retrovirus with thermolabile DNA polymerase were tested for thermal sensitivity of their DNA endonuclease activity. Two pol mutants of Rous sarcoma virus, ts335 and ts337, had thermolabile DNA endonuclease; a temperature-resistant revertant of ts335 had a heat-stable DNA endonuclease. DNA endonuclease is therefore a product of the pol gene and an integral part of the reverse transcriptase. A second class of pol mutants, typified by ts568 and ts553, had thermolabile DNA polymerase, but heat-stable DNA endonuclease.

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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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