Figure 4.
Figure 4. Analysis of the PriS-PriL interface. (a)
Hydrophilic interactions at the PriS-PriL interface. Hydrogen
bonds are yellow dashed lines. The carbonyl groups of Asp162 and
Asp163 at the C terminus of PriS helix 4
are hydrogen-bonded to the main chain amides of PriL residues
Lys165 and Gly166. The side chains of Asp162 and Asp163 further
interact electrostatically with Arg224 and Arg227. (b)
Structure-based yeast two-hybrid analysis of the Sso PriS-PriL
interface. Single and double mutations in PriS and PriL disrupt
the interaction between the core primase subunits. Control
plate: -Leu, -Trp; selective plates: -Leu, -Trp, -His and the
more stringent -Leu, -Trp, -His, -Adenine. Numbered samples are
identified in Table 1.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2005,
12,
1137-1144)
copyright 2005.
4
are hydrogen-bonded to the main chain amides of PriL residues
Lys165 and Gly166. The side chains of Asp162 and Asp163 further
interact electrostatically with Arg224 and Arg227. (b)
Structure-based yeast two-hybrid analysis of the Sso PriS-PriL
interface. Single and double mutations in PriS and PriL disrupt
the interaction between the core primase subunits. Control
plate: -Leu, -Trp; selective plates: -Leu, -Trp, -His and the
more stringent -Leu, -Trp, -His, -Adenine. Numbered samples are
identified in Table 1.