SITE-DIRECTED MUTAGENESIS OF THE CONSERVED ASP-443 AND ASP-498 CARBOXY-TERMINAL RESIDUES OF HIV-1 REVERSE-TRANSCRIPTASE

被引:55
作者
MIZRAHI, V [1 ]
USDIN, MT [1 ]
HARINGTON, A [1 ]
DUDDING, LR [1 ]
机构
[1] UNIV WITWATERSRAND,JOHANNESBURG 2000,SOUTH AFRICA
基金
英国医学研究理事会;
关键词
D O I
10.1093/nar/18.18.5359
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Substitution of the conserved Asp-443 residue of HIV-1 reverse transcriptase by asparagine specifically suppressed the ribonuclease H activity of the enzyme without affecting the reverse transcriptase activity, suggesting involvement of this ionizable residue at the ribonuclease H active site. An analogous asparagine substitution of the Asp-498 residue yielded an unstable enzyme that was difficult to enzymatically characterize. However, the instability caused by the Asn-498 mutation was relieved by the introduction of a second distal Asn-443 substitution, yielding an enzyme with wild type reverse transcriptase activity, but lacking ribonuclease H activity. © 1990 Oxford University Press.
引用
收藏
页码:5359 / 5363
页数:5
相关论文
共 27 条