title: Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function.
abstract: Two single site substitutions (E478----Q and H539----F) were introduced into the C-terminal RNase H domain of HIV-1 reverse transcriptase. These mutant proteins were expressed in Escherichia coli and purified by Ni2+-nitrilotriacetic acid affinity chromatography. Both enzymes are clearly defective in RNase H function, but exhibit wild type reverse transcriptase activity.
authors: Central Research Units, F. Hoffmann-LaRoche Ltd., Basel, Switzerland.
authors: O
authors: O
authors: Schatz
authors: F V
authors: FV
authors: Cromme
authors: F
authors: F
authors: Grüninger-Leitch
authors: S F
authors: SF
authors: Le Grice
mesh_terms: D000595:Amino Acid Sequence; D004252:DNA Mutational Analysis; D004722:Endoribonucleases / Q000378:metabolism*; D015497:HIV-1 / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D012194:RNA-Directed DNA Polymerase / Q000235:genetics / Q000378:metabolism*; D016914:Ribonuclease H; D013329:Structure-Activity Relationship
chemical_list: D012194:RNA-Directed DNA Polymerase; D004722:Endoribonucleases; D016914:Ribonuclease H