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Figure 3
Cloning and purification of RepA and its fragments. (A) Linear sketches of RepA and the fragments cloned, expressed and purified for the studies described in this paper. Dashed vertical lines mark the boundaries for the LZ and HTH motifs, as well as those for the putative domains defined by proteolysis. The location of point mutations that broaden the host range for pPS10 plasmid (*) (Giraldo et al., 1992; Fernández-Tresguerres et al., 1995) are indicated, as well as the unique tryptophane residue (W94) used as a probe in the fluorescence spectroscopy studies (Figure 5). B) SDS–PAGE (15% polyacrylamide) of purified stocks of RepA–WT and its fragments. Molecular weight standards (MW st.) are the same as shown in Figure 2A. Masses for the RepA proteins are: 26.7 kDa (WT), 22.6 kDa ( N37), 22.0 kDa (N42), 11.6 kDa (N132), 11.1 kDa (N37C133) and 15.3 kDa (C133).
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