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. Author manuscript; available in PMC: 2018 Aug 2.
Published in final edited form as: Cell Rep. 2018 Jun 5;23(10):3031–3041. doi: 10.1016/j.celrep.2018.05.020

Figure 4. Replacement of Thymidine with 5-FdUTP Reduces the Binding of POT1-TPP1 to Telomere DNA Sequence.

Figure 4

(A) A representative gel shift used to determine the binding of POT1-TPP1 protein to ssDNA under equilibrium binding conditions. The lower band represents free, radiolabeled ssDNA, and the upper band indicates ssDNA-protein complex.

(B) Gel shift data were quantified and fitted to calculate dissociation constants (KDs) of POT1-TPP1 for several substrates with native thymidine replaced with 5-FdUTP. Data are represented as mean ± SEM (n = 3).

(C) A table summarizing the results indicates that 5-FdUTP exhibits differing positional effects on POT1-TPP1 binding affinity for ssDNA substrates.