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학술저널
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한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제20권 제6호
발행연도
2010.1
수록면
968 - 973 (6page)

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In order to study its biochemical properties, the integrase (IN) protein of feline foamy virus (FFV) was overexpressed in Escherichia coli, purified by two-step chromatography,(Talon column and heparin column), and characterized in biochemical aspects. For the three enzymatic reactions of the 3'-processing, strand transfer, and disintegration activities, the Mn2+ ion was essentially required as a cofactor. Interestingly, Co2+ and Zn2+ ions were found to act as effective cofactors, whereas other transition elements such as Ni2+, Cu2+, La3+, Y3+, Cd2+, Li1+, Ba2+, Sr2+, and V3+were not. Regarding the substrate specificity, FFV IN has low substrate specificities as it cleaved in a significant level prototype foamy virus (PFV) U5 LTR substrate as well as FFV U5 LTR substrate, whereas PFV IN did not. Finally, the 3'-processing activity was observed in high concentrations of several solvents such as CHAPS, glycerol,Tween 20, and Triton X-100, which are generally used for dissolution of chemicals in inhibitor screening. Therefore,in this first report showing its biochemical properties,FFV IN is proposed to have low specificities on the use of cofactor and substrate for enzymatic reaction as compared with other retroviral INs.

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