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. 2009 Aug 20;28(19):2981–2991. doi: 10.1038/emboj.2009.233

Figure 3.

Figure 3

The OB-fold within Pol III α subunit binds ssDNA and is needed for processive synthesis. (A) Scheme of the domain structure of Pol III α subunit. The expanded C-terminal region shows the OB domain and sequences that bind β and τ. (B) Fluorescence anisotropy DNA-binding assay. The isolated wt OB domain (left), or the mutant OB domain (right), is titrated into a reaction containing 5′-fluorescent labelled DNA. (C) Analysis of wt (squares) and OB-mutant (circles) Pol III core (left plot) and Pol III* (right plot) in β-independent assays using gapped DNA. (D) Native agarose gel product analysis of β-dependent replication assays using primed M13mp18 ssDNA and either wt Pol III core (lanes 1–4) or OB-mutant Pol III core (lanes 5–8). (E) As in (D) except using wt Pol III* (lanes 1–6) or OB-mutant Pol III* (lanes 7–12).