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

FEBS Letters

Grüninger-Leitch, Fiona¹  Le Grice, Stuart F.J.¹  Cromme, Frans V.¹  Schatz, Octavian¹ 

[1] Central Research Units, F. Hoffmann-LaRoche Ltd., CH-4002 Basel, Switzerland

关键词: RNase H;    HIV-1 reverse transcriptase;    Site-directed mutagenesis;   

DOI  :  10.1016/0014-5793(89)81559-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown