Department of Biotechnology, Chung-Ang University, Ansung, Korea.
BMB Rep. 2013 Jan;46(1):53-8. doi: 10.5483/bmbrep.2013.46.1.118.
We constructed deletion mutants and seven point mutants by polymerase chain reaction to investigate the specificity of feline foamy virus integrase functional domains. Complementation reactions were performed for three enzymatic activities such as 3'-end processing, strand transfer, and disintegration. The complementation reactions with deletion mutants showed several activities for 3'-end processing and strand transfer. The conserved central domain and the combination of the N-terminal or C-terminal domains increased disintegration activity significantly. In the complementation reactions between deletion and point mutants, the combination between D107V and deletion mutants revealed 3'-end processing activities, but the combination with others did not have any activity, including strand transfer activities. Disintegration activity increased evenly, except the combination with glutamic acid 200. These results suggest that an intact central domain mediates enzymatic activities but fails to show these activities in the absence of the N-terminal or C-terminal domains.
我们通过聚合酶链反应构建了缺失突变体和七个点突变体，以研究猫泡沫病毒整合酶功能域的特异性。我们进行了三种酶活性（3'-末端加工、链转移和分解）的互补反应。缺失突变体的互补反应显示了几种 3'-末端加工和链转移活性。保守的中央结构域和 N 端或 C 端结构域的组合显著增加了分解活性。在缺失和点突变体之间的互补反应中，D107V 与缺失突变体的组合显示出 3'-末端加工活性，但与其他突变体的组合没有任何活性，包括链转移活性。除了与谷氨酸 200 的组合外，分解活性均匀增加。这些结果表明，完整的中央结构域介导酶活性，但在缺乏 N 端或 C 端结构域的情况下无法显示这些活性。
