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Figure 4.
Fig. 4. G526R mutation strengthens dimer interaction. (A)
"Back" view of the GlyRS subunit that shows the dimerization
interface. This view is related to the "front" view in Fig. 1A
by a 180° rotation along the y axis. The three patches that
give dimer interactions are colored: patch 1 (F78–T137) in
cyan, patch 2 (F224–L242) in green, and patch 3 (L252–E291)
in gold. (B) Loose dimerization interface of wild-type GlyRS
generated by mapping the surface area of one subunit that is
within 7 Å of the other. (C) The same dimerization
interface generated for G526R mutant. The extra dimer interface,
absent in the wild-type enzyme, lies in the anticodon
recognition domain and is  30 Å away from the
mutation site. (D) Analytical ultracentrifugation experiment
showing that more dimers are formed by G526R mutant than by
wild-type GlyRS. (Inset) Immunoprecipitation experiment showing
that G526R mutant GlyRS pulled down more endogenous GlyRS than
did the wild-type GlyRS, presumably by forming dimers.
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