Vink C, Yeheskiely E, van der Marel G A, van Boom J H, Plasterk R H
Division of Molecular Biology, The Netherlands Cancer Institute, Amsterdam.
Nucleic Acids Res. 1991 Dec 25;19(24):6691-8. doi: 10.1093/nar/19.24.6691.
Before integration of the human immunodeficiency virus (HIV) DNA, two nucleotides are removed from the 3' ends of the viral DNA by the integrase (IN) protein. We studied the chemistry of this reaction, and found that IN mediates site-specific hydrolysis of a phosphodiester bond, resulting in release of a dinucleotide. A class of alcohols (including glycerol, 1,2-propanediol, but not 1,3-propanediol) can also act as nucleophile in this reaction, and likewise the alcoholic amino acids L-serine and L-threonine can be covalently linked to the dinucleotide. No evidence was found for a covalent linkage between the IN protein and this dinucleotide, suggesting that IN directs a single nucleophilic attack of water at the specific phosphodiester bond.
在人类免疫缺陷病毒（HIV）DNA整合之前，整合酶（IN）蛋白会从病毒DNA的3'末端去除两个核苷酸。我们研究了该反应的化学过程，发现IN介导磷酸二酯键的位点特异性水解，导致二核苷酸的释放。一类醇（包括甘油、1,2-丙二醇，但不包括1,3-丙二醇）也可在该反应中充当亲核试剂，同样，醇性氨基酸L-丝氨酸和L-苏氨酸可与二核苷酸共价连接。未发现IN蛋白与该二核苷酸之间存在共价连接的证据，这表明IN指导水对特定磷酸二酯键进行单次亲核攻击。
