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. 2015 Mar 16;43(7):3776–3788. doi: 10.1093/nar/gkv224

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Molecular determinant of mimiviruses PAP dimerization and processivity. (A) Mg561 dimer symmetry. Rotational symmetry axis is shown in gray. Figure 1 color code is applied to one monomer and the second monomer is in light gray. (B) Buried surface area of the Mg561 dimer. The dimer interface buries a surface area (yellow) of about 3200 Å², which corresponds to 11.5% of each monomer's solvent accessible surface area (about 27 500 Å²). The first monomer is in cyan, the second one is in magenta. Cation locations are marked as green balls. (C) Gel filtration analysis of ΔD1 H₆c-Mg561 and ΔD1 H₆c-R341 mutants. Overlay of UV traces of the full-length H₆c-Mg561 (dark blue curve) and ΔD1 H₆c-Mg561 (light blue curve) proteins (Left panel) and of the full-length H₆c-R341 (dark green curve) and ΔD1 H₆c-R341 (light green curve) proteins (Right panel). Full-length H₆c-Mg561 and H₆c-R341 eluted as a single peak corresponding to a dimeric state: apparent molecular masses were 116.8 and 176.7 kDa, respectively, versus the calculated ones, 125.7 and 136.8 kDa. At least 90% of the ΔD1 H₆c-Mg561 and ΔD1 H₆c-R341 protein eluted as monomers: apparent molecular masses were 57.8 and 71.1 kDa versus the calculated 57.7 and 63.4 kDa. GE Healthcare markers were used for calibration. (D) PolyA polymerase assay of H₆c-Mg561, ΔD1 H₆c-Mg561, H₆c-R341 and ΔD1 H₆c-R341 on a 20-mers RNA primer in the presence of Mg²⁺ or Mn²⁺ as catalytic ions. Time course is in min.