Unwinding of a DNA replication fork by a hexameric viral helicase

Abid Javed, Balazs Major, Jonathan A. Stead, Cyril M. Sanders () and Elena V. Orlova ()
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Abid Javed: Institute of Structural and Molecular Biology
Balazs Major: Medical School
Jonathan A. Stead: Medical School
Cyril M. Sanders: Medical School
Elena V. Orlova: Institute of Structural and Molecular Biology

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Hexameric helicases are motor proteins that unwind double-stranded DNA (dsDNA) during DNA replication but how they are optimised for strand separation is unclear. Here we present the cryo-EM structure of the full-length E1 helicase from papillomavirus, revealing all arms of a bound DNA replication fork and their interactions with the helicase. The replication fork junction is located at the entrance to the helicase collar ring, that sits above the AAA + motor assembly. dsDNA is escorted to and the 5´ single-stranded DNA (ssDNA) away from the unwinding point by the E1 dsDNA origin binding domains. The 3´ ssDNA interacts with six spirally-arranged β-hairpins and their cyclical top-to-bottom movement pulls the ssDNA through the helicase. Pulling of the RF against the collar ring separates the base-pairs, while modelling of the conformational cycle suggest an accompanying movement of the collar ring has an auxiliary role, helping to make efficient use of ATP in duplex unwinding.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25843-6

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DOI: 10.1038/s41467-021-25843-6

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