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.
Restle
T
T
Abteilung Biophysik, Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany.
Müller
B
B
Goody
R S
RS
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