ATP-induced helicase slippage reveals highly coordinated subunits

Bo Sun, Daniel S. Johnson, Gayatri Patel, Benjamin Y. Smith, Manjula Pandey, Smita S. Patel () and Michelle D. Wang ()
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Bo Sun: Cornell University
Daniel S. Johnson: Cornell University
Gayatri Patel: UMDNJ-Robert Wood Johnson Medical School
Benjamin Y. Smith: Cornell University
Manjula Pandey: UMDNJ-Robert Wood Johnson Medical School
Smita S. Patel: UMDNJ-Robert Wood Johnson Medical School
Michelle D. Wang: Cornell University

Nature, 2011, vol. 478, issue 7367, 132-135

Abstract: When ATP is not enough Most helicases — ubiquitous motor proteins that catalyse strand separation of base-paired nucleic acids — use ATP as an energy source. The hexameric helicase of T7 bacteriophage, the gene 4 protein, does not unwind DNA efficiently in the presence of ATP but instead uses deoxythymine triphosphate (dTTP). Using a single-molecule approach, Michelle Wang and colleagues show that with this helicase, ATP allows repeated slips during unwinding that prevent unwinding over any significant distance. This behaviour is not observed with dTTP. Using these two nucleotides, they show that the six subunits act together to coordinate nucleotide binding and hydrolysis in a way that promotes processive unwinding of the DNA.

Date: 2011
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DOI: 10.1038/nature10409

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