Fig. 4.
Fig. 4. HDAC3 does not alter DNA-binding activity of GATA-2. / Nuclear extracts from COS cells transfected with GATA-2 expression vector (Flag–GATA-2) in the presence or absence of HDAC3 expression vector (Myc-HDAC3) were used in EMSAs. A 32P-labeled double-stranded oligonucleotide containing a GATA consensus recognition site was used as a probe. The protein-DNA complex was revealed in lanes 2 and 4. Competitive experiments were performed using a 2000-fold excess of the unlabeled oligonucleotide (lane 3). Supershift experiments were performed by addition of α-Flag antibody, with the combination α-GATA-1 antibody serving as a control, as indicated. Specific GATA-2–DNA complexes and the supershifted complexes are indicated. The supershifted band by α-Flag antibody is denoted with an asterisk.

HDAC3 does not alter DNA-binding activity of GATA-2.

Nuclear extracts from COS cells transfected with GATA-2 expression vector (Flag–GATA-2) in the presence or absence of HDAC3 expression vector (Myc-HDAC3) were used in EMSAs. A 32P-labeled double-stranded oligonucleotide containing a GATA consensus recognition site was used as a probe. The protein-DNA complex was revealed in lanes 2 and 4. Competitive experiments were performed using a 2000-fold excess of the unlabeled oligonucleotide (lane 3). Supershift experiments were performed by addition of α-Flag antibody, with the combination α-GATA-1 antibody serving as a control, as indicated. Specific GATA-2–DNA complexes and the supershifted complexes are indicated. The supershifted band by α-Flag antibody is denoted with an asterisk.

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