PMID: 6163872Feb 1, 1981Paper

Mechanism of action of Moloney murine leukemia virus RNase H III

Journal of Virology
G F Gerard

Abstract

The mechanism of action of Moloney murine leukemia virus RNase H III was studied, utilizing the model substrate (A)n. (dT)n and polyacrylamide gel electrophoresis to assay enzyme activity. Examination by electrophoresis on 15% polyacrylamide gels in 7 M urea and on DEAE-cellulose paper in 7 M urea revealed that, early in a reaction with [3H](A)n. (dT)n as substrate, RNase H III generated products ranging in length from 80 to 90 nucleotides to less than 10 nucleotides and that after extended incubation the limit digest products generated were 3 to 15 nucleotides long. Product oligomers were of the following configuration: [5'-P, 3'-OH](A)n. RNase H III was shown to be an exonuclease requiring free ends in its substrate for activity by the inability to degrade RNA inserted in Escherichia coli ColE1 plasmid DNA. The enzyme was capable of attacking RNA in RNA-DNA hybrids in the 5' to 3' and 3' to 5' directions as demonstrated by the use of [3H, 5'-32P](A)600. (dT)n and cellulose-[3H](A)n. (dT)n. Rnase H III was random in its mode of action because addition of excess unlabeled (A)n. (dT)n to an ongoing reaction with [3H](A)n. (dT)n as substrate resulted in immediate inhibition of enzyme activity.

References

Apr 1, 1978·Journal of Virology·G F Gerard
Sep 1, 1978·Journal of Virology·M H LaiS A Aaronson
Dec 1, 1972·Journal of Virology·D P GrandgenettM Green
Feb 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·J P LeisJ Hurwitz
Sep 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·J G StavrianopoulosE Chargaff
Apr 14, 1969·Journal of Molecular Biology·A E DahlbergA C Peacock

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