Figure 6 - full size

 

Figure 6.
Figure 6. Interaction of the Sso core primase with DNA template and RNA primer. (a) The zinc-binding motif of archaeal primases. The small subunits of Sso, Pho (PDB entry 1V33) and Sis (PDB entry 1RNI) primases were superimposed. The Sso PriS-prim is shown as a molecular surface. The zinc-binding motifs of Sso (green), Pho (yellow) and Sis (pink) are narrow tubes and their zinc atoms are spheres. (b) Comparison of the enzymatic activity of wild-type Sso core primase (Pri-WT) with that of the RR and SNG mutants (Pri-RR and Pri-SNG, respectively). Experiments were performed as for Figure 1c. DN, dinucleotide product. (c) Comparison of the quantities of product synthesized by Pri-WT and the RR and SNG mutants. Experiments were performed as for Figure 1c, with 1.2 M primase concentration. The radiolabeled products were quantified by filter binding and liquid scintillation counting. Each bar represents the average of five independent values with s.e.m. indicated. (d) Model of the Sso core primase-DNA template-RNA primer complex. The protein component of the complex is depicted as a molecular surface. The phosphate backbones of DNA and RNA are orange and cyan tubes, respectively. The proposed trajectory of the template DNA across the surface of the core primase is drawn. The position of PriS-Zn and the putative position of PriL-CTD are indicated by solid and dashed circles, respectively. The side chains of basic residues on and near PriL 5 are blue. The positions of PriL residues Arg84 and Arg85 are indicated.

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2005, 12, 1137-1144) copyright 2005.