HIV-1逆转录酶C末端结构域内保守氨基酸残基的点突变会特异性抑制核糖核酸酶H的功能。
Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function.
作者信息
Schatz O, Cromme F V, Grüninger-Leitch F, Le Grice S F
机构信息
Central Research Units, F. Hoffmann-LaRoche Ltd., Basel, Switzerland.
出版信息
FEBS Lett. 1989 Nov 6;257(2):311-4. doi: 10.1016/0014-5793(89)81559-5.
PMID:2479577
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.
摘要
两个单一位点取代（E478----Q和H539----F）被引入到HIV-1逆转录酶的C端核糖核酸酶H结构域。这些突变蛋白在大肠杆菌中表达，并通过镍离子-次氮基三乙酸亲和色谱法进行纯化。这两种酶在核糖核酸酶H功能上均明显存在缺陷，但表现出野生型逆转录酶活性。
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