Fig. 2 | Nature Communications

Fig. 2

From: Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity

Fig. 2

Shelterincore complex binds strongest to telomeric DNA with both single-stranded and double-stranded regions. a Representative Ag-EMSA shows shelterincore complex binding to a telomeric DNA substrate (C8) with binding sites for both TRF2 dimer and POT1 and to C8mutTRF and C8mutPOT1, which have mutated TRF2 dimer and POT1-binding sites, respectively. b The equilibrium dissociation constants (K d,app) were determined through curve fitting (with Hill equation) from the Ag-EMSA gels. Error bars represent s.d. (n = 3 independent experiments). c Binding affinity increases some what with increasing spacer length (base pairs) between TRF2 dimer and POT1-binding sites. (Error bars are s.d., n = 3 independent experiments.)

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