TY - JOUR
T1 - RNase H and RNA directed DNA polymerase
T2 - associated enzymatic activities of murine mammary tumor virus
AU - Dion, A. S.
AU - Williams, C. J.
AU - Moore, D. H.
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1977
Y1 - 1977
N2 - The RNA-directed DNA polymerase of murine mammary tumor virus, a type B RNA tumor virus, was purified sequentially through DEAE-cellulose, phosphocellulose (step gradient), and phosphocellulose (linear salt gradient) chromatography, followed by glycerol sedimentation centrifugation. During all stages of purification, coincident peaks of RNA-directed DNA polymerase activity, templated by polyribocytidylate.oligodeoxyguanidylate, and RNase H digestion of [3H]polyriboadenylate.polydeoxythymidylate were observed, and both enzymatic activities displayed a cation preference for magnesium. Under conditions that removed adventitiously associated nucleases, RNase H activity was found to co-purify with polymerase. The specificity of this nuclease was assayed with various prepared substrates, which indicated that the polymerase-associated RNase H activity was directed only against the RNA strand of an RNA.DNA hybrid. It is highly probable that RNase H (RNA.DNA hybrid: ribonucleotide-hydrolase) and RNA-directed DNA polymerase of type B viruses are associated enzymatic activities analogous to those observed for avian and mammalian type C RNA tumor viruses.
AB - The RNA-directed DNA polymerase of murine mammary tumor virus, a type B RNA tumor virus, was purified sequentially through DEAE-cellulose, phosphocellulose (step gradient), and phosphocellulose (linear salt gradient) chromatography, followed by glycerol sedimentation centrifugation. During all stages of purification, coincident peaks of RNA-directed DNA polymerase activity, templated by polyribocytidylate.oligodeoxyguanidylate, and RNase H digestion of [3H]polyriboadenylate.polydeoxythymidylate were observed, and both enzymatic activities displayed a cation preference for magnesium. Under conditions that removed adventitiously associated nucleases, RNase H activity was found to co-purify with polymerase. The specificity of this nuclease was assayed with various prepared substrates, which indicated that the polymerase-associated RNase H activity was directed only against the RNA strand of an RNA.DNA hybrid. It is highly probable that RNase H (RNA.DNA hybrid: ribonucleotide-hydrolase) and RNA-directed DNA polymerase of type B viruses are associated enzymatic activities analogous to those observed for avian and mammalian type C RNA tumor viruses.
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U2 - 10.1128/jvi.22.1.187-193.1977
DO - 10.1128/jvi.22.1.187-193.1977
M3 - Article
C2 - 67221
AN - SCOPUS:0017350838
VL - 22
SP - 187
EP - 193
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 1
ER -