Article
Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase.
The EMBO journal - 1 Dec 1991
Le Grice S F, Naas T, Wohlgensinger B, Schatz O
Abstract excerpt
We have purified and determined functional parameters of reconstituted, recombinant HIV-1 reverse transcriptase (RT) heterodimers within which either the p66 or p51 polypeptide was selectively mutated in one or both aspartic acid residues constituting the proposed polymerase active site (-Y-M-D-D-). Heterodimers containing a mutated p51 polypeptide retain almost wild type levels of both RNA-dependent DNA...
Topics
- Binding Sites
- Chromatography, Ion Exchange
- DNA-Directed DNA Polymerase
- Electrophoresis, Polyacrylamide Gel
- HIV-1
- Mutagenesis, Site-Directed
- Mutation
- Plasmids
- RNA-Directed DNA Polymerase
- Ribonuclease H