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. 2005 Aug 1;33(13):4285–4310. doi: 10.1093/nar/gki720

Figure 5.

Figure 5

Sp proteins bind to the GC-box located in the HS7 region. (A) The nucleotide sequence of the wild-type Sp site oligonucleotide is aligned with the Sp1 consensus sequence. The GC-box present in the Sp site is indicated by an arrow and the recognition core sequence 5′-GG-3′ is indicated by a thicker bar. (B) The HS7 Sp wt site oligonucleotide probe was incubated with 15 μg of nuclear extracts from Jurkat cells in the absence of competitor (lane 1) or in the presence of increasing concentrations (25-, 50-, 100- or 200-fold molar excess) of the homologous HS7 Sp site wt oligonucleotide (lanes 2–5), of the Sp1 consensus oligonucleotide (lanes 6–9), of a mutated Sp1 consensus oligonucleotide (lanes 10–13) or of the heterologous HS7 site B oligonucleotide (lanes 14–17). The sequence of the coding strand of the Sp1 consensus oligonucleotide and the sequence of the mutated Sp1 consensus oligonucleotide were as follows: 5′-ATTCGATCGGGGCGGGGCGAG-3′ and 5′-ATTCGATCGGTTCGGGGCGAGC-3′, respectively. The figure shows only the specific retarded bands of interest. The two retarded DNA–protein complexes are indicated by arrows. (C) Nuclear extracts from Jurkat cells (15 μg) were incubated in the absence of antibody or in the presence of antibodies directed against MEF-2, Sp1 and/or Sp3 (as indicated at the top of each lane) before the addition of the HS7 Sp wt site oligonucleotide probe. The figure shows only the specific retarded bands. The retarded DNA–protein complexes and the supershifted complexes are indicated by arrows.