Loya S, Gao H Q, Avidan O, Boyer P L, Hughes S H, Hizi A
Department of Cell Biology and Histology, Sackler School of Medicine, Tel Aviv University, Israel.
J Virol. 1997 Jul;71(7):5668-72. doi: 10.1128/JVI.71.7.5668-5672.1997.
Treatment of human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) with N-ethylmaleimide (NEM) selectively inhibits the RNase H activity. The cysteine residue at position 280 (C280) is the target for NEM; HIV-1 RT carrying the mutation C280S is resistant to NEM. Since HIV-1 RT is composed of two related subunits (p66 and p51) that play distinct roles, we asked whether the C280 in p51 or the C280 in p66 is responsible for the sensitivity of the enzyme to NEM. HIV-1 RT versions were prepared that had one mutant and one wild-type subunit. When these chimeric enzymes were tested, both the p51 and p66 subunits were found to contribute to the sensitivity of the enzyme to NEM. The implications of these results are discussed in the context of the structure of the enzyme.
用N - 乙基马来酰亚胺（NEM）处理1型人类免疫缺陷病毒逆转录酶（HIV-1 RT）可选择性抑制核糖核酸酶H活性。第280位的半胱氨酸残基（C280）是NEM的作用靶点；携带C280S突变的HIV-1 RT对NEM具有抗性。由于HIV-1 RT由两个发挥不同作用的相关亚基（p66和p51）组成，我们探究是p51中的C280还是p66中的C280导致该酶对NEM敏感。制备了具有一个突变亚基和一个野生型亚基的HIV-1 RT变体。对这些嵌合酶进行测试时，发现p51和p66亚基均对该酶对NEM的敏感性有影响。结合该酶的结构对这些结果的意义进行了讨论。
