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Structural study of the function of Candida Albicans Pif1.
Biochem Biophys Res Commun, 567:190-194.
Pif1 helicases, conserved in eukaryotes, are involved in maintaining genomestability in both the nucleus and mitochondria. Here, we report the crystalstructure of a truncated Candida Albicans Pif1 (CaPif1(368-883)) in complex withssDNA and an ATP analog. Our results show that the Q-motif is responsible foridentifying adenine bases, and CaPif1 preferentially utilizes ATP/dATP duringdsDNA unwinding. Although CaPif1 shares structural similarities withSaccharomyces cerevisiae Pif1, CaPif1 can contact the thymidine bases of DNA byhydrogen bonds, whereas ScPif1 cannot. More importantly, the crosslinking andmutant experiments have demonstrated that the conformational change of domain 2Bis necessary for CaPif1 to unwind dsDNA. These findings contribute to further theunderstanding of the unwinding mechanism of Pif1.
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