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KMID : 0370220050490030198
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Yakhak Hoeji
2005 Volume.49 No. 3 p.198 ~ p.204
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Characterization of Human Foamy Virus Integrase Mutant
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배정우/Bae JW
김현경/양상인/김지홍/김경혜/장춘곤/박영서/손의동/이석용/Kim HK/Yang SI/Kim JH/Kim KH/Jang CG/Park YS/Sohn UD/Lee SY
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Abstract
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Human foamy virus (HFV) integrase mediates integration of viral c-DNA into cellular DNA. In this process, HFV integrase recognizes its own viral DNA specifically and catalyzes insertion of viral c-DNA. In order to study catalytic domains and residues, three deletion mutants and two point mutants of HFV integrase were constructed and analyzed with respect to enzymatic activities. The C-terminal deletion mutant showed decreased enzymatic activities while the N-terminal deletion mutant lost the activities completely, indicating that the N-terminal domain is more important than the C-terminal domain enzymatic reaction. The point mutants, in which an aspartic acid at the 164th position or a glutamic acid at the 200th position of The HFV integrase protein was changed to alanine, lost the enzymatic activities completely. However, they results suggest that the aspartic acid and glutamic acid at the respective 164th and 200th positions are catalytic residues for enzymatic reaction.
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KEYWORD
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