Cloning and characterization of hELD/OSA1, a novel BRG1 interacting protein.

A highly conserved multisubunit enzymic complex, SWI/SNF, participates in the regulation of eukaryote gene expression through its ability to remodel chromatin. While a single component of SWI/SNF, Swi2 or a related protein, can perform this function in vitro, the other components appear to modulate the activity and specificity of the ...
complex in vivo. Here we describe the cloning of hELD/OSA1, a 189 KDa human homologue of Drosophila Eld/Osa protein, a constituent of Drosophila SWI/SNF. By comparing conserved peptide sequences in Eld/Osa homologues we define three domains common to all family members. A putative DNA binding domain, or ARID (AT-rich DNA-interacting domain), may function in targetting SWI/SNF to chromatin. Two other domains unique to Eld/Osa proteins, EHD1 and EHD2, map to the C-terminus. We show that EHD2 mediates binding to Brahma-related gene 1 (BRG1), a human homologue of yeast Swi2. EHD1 and EHD2 also appear capable of interacting with each other. Using an antibody raised against EHD2 of hELD/OSA1, we detected Eld/Osa1 in endogenous SWI/SNF complexes derived from mouse brain.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Animals, Antibodies, Monoclonal, Base Sequence, COS Cells, Cattle, Chromatin, Cloning, Molecular, DNA, DNA Helicases, DNA, Complementary, DNA-Binding Proteins, Drosophila, Epitopes, Humans, Immunoblotting, Mice, Molecular Sequence Data, Nuclear Proteins, Peptides, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Transcription Factors, Transfection, Two-Hybrid System Techniques
Biochem. J.
Date: May. 15, 2002
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