Redesignation of the RNase D activity associated with retroviral reverse transcriptase as RNase H
Zdeněk Hostomský, S H Hughes, Stephen P. Goff, S F Le Grice
Abstract
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Zdeněk Hostomský, S H Hughes, Stephen P. Goff, S F Le Grice
Abstract
Open-access reader
In the presence of Mn2+, reverse transcriptase of both human immunodeficiency virus and murine leukemia virus hydrolyzes duplex RNA. However, designating this novel activity RNase D conflicts with Escherichia coli RNase D, which participates in tRNA processing. On the basis of its location in the RNase H domain, we propose that this novel retroviral activity be redesignated RNase H*.
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In the presence of Mn2+, reverse transcriptase of both human immunodeficiency virus and murine leukemia virus hydrolyzes duplex RNA. However, designating this novel activity RNase D conflicts with Escherichia coli RNase D, which participates in tRNA processing. On the basis of its location in the RNase H domain, we propose that this novel retroviral activity be redesignated RNase H*.
Key concepts: RNase H, Reverse transcriptase, RNase MRP, Biology, RNase P, Murine leukemia virus, Ribonuclease III, RNase PH