Fig. 4.
Fig. 4. Erythropoietin 5′-UTR recruits a methyl-CpG–binding protein. / Electrophoretic mobility shift assays were performed with methylated and unmethylated CG11 and EPO236 as probes and competitors. [32P]-end-labeled probes were incubated with nuclear extracts and, where indicated, with excess unlabeled competitors. (A) CG11 probe. (B) EPO236 probe. U, unmethylated; M, methylated probe or competitor. Probe identity and methylation status are noted below the panels, and competitors and sources of nuclear extracts are noted above the panels. (arrow) Methyl-CpG–binding complex. (asterisks) Complexes formed on unmethylated probes blocked by methylation. (arrowheads) Protein complexes formed on unmethylated and methylated probes, whose formation is blocked by methylated and unmethylated competitors.

Erythropoietin 5′-UTR recruits a methyl-CpG–binding protein.

Electrophoretic mobility shift assays were performed with methylated and unmethylated CG11 and EPO236 as probes and competitors. [32P]-end-labeled probes were incubated with nuclear extracts and, where indicated, with excess unlabeled competitors. (A) CG11 probe. (B) EPO236 probe. U, unmethylated; M, methylated probe or competitor. Probe identity and methylation status are noted below the panels, and competitors and sources of nuclear extracts are noted above the panels. (arrow) Methyl-CpG–binding complex. (asterisks) Complexes formed on unmethylated probes blocked by methylation. (arrowheads) Protein complexes formed on unmethylated and methylated probes, whose formation is blocked by methylated and unmethylated competitors.

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