Journal
CELL REPORTS
Volume 14, Issue 8, Pages 2030-2039Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2016.02.008
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Funding
- Natural Science Foundation of China [31470723]
- Agency for Science, Technology and Research in Singapore
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Pif1 is a conserved SF1B DNA helicase involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. Here, we report the structures of the helicase domain of human Pif1 and Bacteroides sp Pif1 (BaPif1) in complex with ADP-AlF4- and two different single-stranded DNAs (ssDNAs). The wedge region equivalent to the b hairpin in other SF1B DNA helicases folds into an extended loop followed by an alpha helix. The Pif1 signature motif of BaPif1 interacts with the wedge region and a short helix in order to stabilize these ssDNA binding elements, therefore indirectly exerting its functional role. Domain 2B of BaPif1 undergoes a large conformational change upon concomitant binding of ATP and ssDNA, which is critical for Pif1's activities. BaPif1 cocrystallized with a tailed dsDNA and ADP-AlF4-, resulting in a bound ssDNA bent nearly 90 degrees at the ssDNA/dsDNA junction. The conformational snapshots of BaPif1 provide insights into the mechanism governing the helicase activity of Pif1.
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