SALL4B-bound proteins include the components of Mi-2/NuRD complex.

<p>Extracts from 293Tcells expressing FLAG-SALL4B or mock vector only were immunoprecipitated with anti-FLAG M2 agarose. SALL4B-bound proteins were fractionated by SDS-PAGE, detected by silver staining and identified by tandem mass spectrometry.</p

Transcriptional repression by tethered SALL4B.

<p>(A) Schematic representation of the GAL4 fusion protein (GAL4–SALL4B) and luciferase reporters (GAL4-tk-Luc). 5×Gal4, five copies of the GAL4-binding site; tk, thymidine kinase core promoter. (B) Constructs expressing SALL4B fused to the C-terminus of GAL4 (1–93) were transfected into 293T cells, along with the reporter GAL-tk-Luc. Luciferase activities were normalized to the internal ß-galactosidase control. Different molar ratios of GAL4-SALL4B and GAL4-tk-Luc were used for transfection.</p

SALL4 associates with Mi-2/NuRD complex and SALL4-interacting protein complex exhibits histone deacetylase (HDAC) activity.

<p>Extracts from SALL4B-expressed 293T cells (A), SALL4B-expressed 293T cells (B), or mouse ES cells, (C) were immunoprecipated with an anti-SALL4 antibody or rabbit IgG control followed by Western blotting with indicated antibodies. The HDAC activity of SALL4-bound protein complex was measured using the fluorimetric assay with or without the TSA (D). Data represent at least two independent experiments. Error bars denote standard deviation (SD).</p