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

O Schatz; F V Cromme; F Grüninger-Leitch; S F Le Grice

doi:10.1016/0014-5793(89)81559-5

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

FEBS Lett. 1989 Nov 6;257(2):311-4. doi: 10.1016/0014-5793(89)81559-5.

Authors

O Schatz¹, F V Cromme, F Grüninger-Leitch, S F Le Grice

Affiliation

¹ Central Research Units, F. Hoffmann-LaRoche Ltd., Basel, Switzerland.

PMID: 2479577
DOI: 10.1016/0014-5793(89)81559-5

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.

MeSH terms

Amino Acid Sequence
DNA Mutational Analysis
Endoribonucleases / metabolism*
HIV-1 / enzymology*
HIV-1 / genetics
Molecular Sequence Data
RNA-Directed DNA Polymerase / genetics
RNA-Directed DNA Polymerase / metabolism*
Ribonuclease H
Structure-Activity Relationship

Substances

RNA-Directed DNA Polymerase
Endoribonucleases
Ribonuclease H