Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function

Two single site substitutions (E 478 → Q and H 539 → 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 Ni 2+-nitrilotriacetic acid affinity chromatography. Both enzymes are clearly defective...

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Bibliographic Details
Published in:FEBS Letters 1989-11, Vol.257 (2), p.311-314
Main Authors: Schatz, Octavian, Cromme, Frans V., Grüninger-Leitch, Fiona, Le Grice, Stuart F.J.
Format: Article
Language:English
Subjects:
AIDS/HIV
Amino Acid Sequence
DNA Mutational Analysis
Endoribonucleases - metabolism
HIV-1 - enzymology
HIV-1 - genetics
HIV-1 reverse transcriptase
Molecular Sequence Data
Ribonuclease H
RNA-Directed DNA Polymerase - genetics
RNA-Directed DNA Polymerase - metabolism
RNase H
Site-directed mutagenesis
Structure-Activity Relationship
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Summary:Two single site substitutions (E 478 → Q and H 539 → 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 Ni 2+-nitrilotriacetic acid affinity chromatography. Both enzymes are clearly defective in RNase H function, but exhibit wild type reverse transcriptase activity.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)81559-5