Table 1. Effects of PapG C‐terminal mutations
PapG variantPapF–G complex stabilityaPapD bindingb
Wild‐type▪▪▪▪●●●●
M307S▪▪▪
M307T▪▪▪
M307PN/A●●
M309A▪▪▪▪
M309S
M309PN/A
L311A▪▪▪
L311S▪▪
L311T▪▪▪●●
F313G▪▪▪▪
F313L▪▪▪▪●●●
F313M▪▪▪▪●●●
F313A▪▪▪▪
F313V▪▪▪▪●●
F313N▪▪▪▪
  • a Relative stability of PapG–PapF interaction compared with wild‐type PapG, as measured by the temperature required to achieve complete dissociation of PapG–PapF complexes. Each block (▪) represents the number of temperature increments (shown in Figure 2B) above 42°C required for complete dissociation [e.g. four blocks indicate that all PapG ran as a monomer by lane 8 (71°C)]. ‘N/A’ signifies that enough material could not be purified from the specified construct in order to perform the experiment.

  • b Relative binding to PapD compared with wild‐type PapG, as measured by ELISA using a PapG–MBP fusion protein. Each dot (●) represents ∼25% binding capacity of wild‐type at the highest concentration studied.