RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

doi:doi:10.1038/nature04331

From the following article:

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

Sophie Dumont, Wei Cheng, Victor Serebrov, Rudolf K. Beran, Ignacio Tinoco, Jr, Anna Marie Pyle and Carlos Bustamante

Nature 439, 105-108 (5 January 2006)

doi:10.1038/nature04331

BACK TO ARTICLE

Download plugins and applications

Supplementary Figures

Eight figures showing a variety of NS3 behaviours (Supplementary Figure 1), that the 11 bp step size is intrinsic to NS3 (Supplementary Figures 2 and 3), that two kinetic events are required for NS3 pause exit (Supplementary Figure 4), that NS3 steps consist of rapid 2–5 bp substeps (Supplementary Figure 5), and providing part of the evidence that NS3 acts as a monomer in the present assay (Supplementary Figures 6, 7 and 8).

Supplementary Figures - Download PDF file (904KB)

Supplementary Discussion

Discussions on the variability in the step size of NS3; the comparison between bulk and single molecule experiments on both theoretical and experimental grounds; the evidence for a single active NS3 monomer; two inchworm model orientations consistent with the data; the role of ATP in coordinating translocator and helix opener movement; thermodynamic considerations on coupling between ATP and duplex unwinding; confirming substrate pairing, geometry and attachment; instrument resolution; and the effects of NS3 binding to the substrate.

Supplementary Discussion - Download PDF file (188KB)

BACK TO ARTICLE