Bypass of a protein barrier by a replicative DNA helicase

Hasan Yardimci, Xindan Wang, Anna B. Loveland, Inger Tappin, David Z. Rudner, Jerard Hurwitz, Antoine M. van Oijen () and Johannes C. Walter ()
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Hasan Yardimci: Harvard Medical School
Xindan Wang: Harvard Medical School
Anna B. Loveland: Harvard Medical School
Inger Tappin: Program of Molecular Biology, Memorial Sloan–Kettering Cancer Center
David Z. Rudner: Harvard Medical School
Jerard Hurwitz: Program of Molecular Biology, Memorial Sloan–Kettering Cancer Center
Antoine M. van Oijen: The Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands
Johannes C. Walter: Harvard Medical School

Nature, 2012, vol. 492, issue 7428, 205-209

Abstract: Abstract Replicative DNA helicases generally unwind DNA as a single hexamer that encircles and translocates along one strand of the duplex while excluding the complementary strand (known as steric exclusion). By contrast, large T antigen, the replicative DNA helicase of the simian virus 40 (SV40), is reported to function as a pair of stacked hexamers that pumps double-stranded DNA through its central channel while laterally extruding single-stranded DNA. Here we use single-molecule and ensemble assays to show that large T antigen assembled on the SV40 origin unwinds DNA efficiently as a single hexamer that translocates on single-stranded DNA in the 3′-to-5′ direction. Unexpectedly, large T antigen unwinds DNA past a DNA–protein crosslink on the translocation strand, suggesting that the large T antigen ring can open to bypass bulky adducts. Together, our data underscore the profound conservation among replicative helicase mechanisms, and reveal a new level of plasticity in the interactions of replicative helicases with DNA damage.

Date: 2012
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DOI: 10.1038/nature11730

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