Two related ARID family proteins are alternative subunits of human SWI/SNF complexes

Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Biochemical Journal (Impact Factor: 4.4). 11/2004; 383(Pt 2):319-25. DOI: 10.1042/BJ20040524
Source: PubMed


p270 (ARID1A) is a member of the ARID family of DNA-binding proteins and a subunit of human SWI/SNF-related complexes, which use the energy generated by an integral ATPase subunit to remodel chromatin. ARID1B is an independent gene product with an open reading frame that is more than 60% identical with p270. We have generated monoclonal antibodies specific for either p270 or ARID1B to facilitate the investigation of ARID1B and its potential interaction with human SWI/SNF complexes in vivo. Immunocomplex analysis provides direct evidence that endogenous ARID1B is associated with SWI/SNF-related complexes and indicates that p270 and ARID1B, similar to the ATPase subunits BRG1 and hBRM, are alternative, mutually exclusive subunits of the complexes. The ARID-containing subunits are not specific to the ATPases. Each associates with both BRG1 and hBRM, thus increasing the number of distinct subunit combinations known to be present in cells. Analysis of the panels of cell lines indicates that ARID1B, similar to p270, has a broad tissue distribution. The ratio of p270/ARID1B in typical cells is approx. 3.5:1, and BRG1 is distributed proportionally between the two ARID subunits. Analysis of DNA-binding behaviour indicates that ARID1B binds DNA in a non-sequence-specific manner similar to p270.

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Available from: Peter Dallas, Nov 10, 2014
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    • "They also comprise the PHD (plant homeobox domain) and zinc finger C5HC2 domains. It is known that KDM5B enzyme is included in many chromatin modifying complexes, such as the nucleosome remodelling and deacetylase complex (NuRD) [151] [152], PRC2 complex [153], and SWI/SNF complex [154]. KDM5B is a potent inhibitor of gene expression not only through the demethylase domain but it also interacts with histone deacetylases (HDAC), those of class I and IIa HDACs [152] [155]. "
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