RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms.
A method for the rapid preparation of a defined substrate to monitor RNase H activity has been developed. Using this substrate, we have investigated the RNase H activities of the different forms of recombinant HIV-1 and HIV-2 reverse transcriptase (RT) in detail. As we report here, RNase H activity is associated only with the dimeric forms (p51/p66 or p66/p66) of the enzymes.
Abteilung Biophysik, Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany.
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T
Restle
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B
Müller
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Goody
D000595:Amino Acid Sequence; D006678:HIV / Q000201:enzymology*; D008969:Molecular Sequence Data; D012194:RNA-Directed DNA Polymerase / Q000737:chemistry / Q000378:metabolism*; D016914:Ribonuclease H / Q000378:metabolism*
D012194:RNA-Directed DNA Polymerase; D016914:Ribonuclease H