Biochemical characteristics of functional domains using feline foamy virus integrase mutants
We constructed deletion mutants and seven point mutants bypolymerase chain reaction to investigate the specificity of felinefoamy virus integrase functional domains. Complementationreactions were performed for three enzymatic activities such as3’-end processing, strand transfer, and disintegration....
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Korean Society for Biochemistry and Molecular Biology
2013-01-01
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| Series: | BMB Reports |
| Subjects: | |
| Online Access: | http://bmbreports.org/jbmb/pdf.php?data=MTMwOTI2MTZAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni0xJTVEMTMwMTI5MjExOV8lMjgwNTMtMDU4JTI5Qk1CXzEyLTExOC5wZGY= |
| Summary: | We constructed deletion mutants and seven point mutants bypolymerase chain reaction to investigate the specificity of felinefoamy virus integrase functional domains. Complementationreactions were performed for three enzymatic activities such as3’-end processing, strand transfer, and disintegration. Thecomplementation reactions with deletion mutants showedseveral activities for 3’-end processing and strand transfer. Theconserved central domain and the combination of the N-terminalor C-terminal domains increased disintegration activitysignificantly. In the complementation reactions between deletionand point mutants, the combination between D107V anddeletion mutants revealed 3’-end processing activities, but thecombination with others did not have any activity, includingstrand transfer activities. Disintegration activity increased evenly,except the combination with glutamic acid 200. These resultssuggest that an intact central domain mediates enzymaticactivities but fails to show these activities in the absence of theN-terminal or C-terminal domains. [BMB Reports 2013; 46(1):53-58] |
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| ISSN: | 1976-6696 1976-670X |