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Molecular and Cellular Biology, May 2000, p. 3137-3146, Vol. 20, No. 9
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Human SWI-SNF Complex Protein p270 Is an ARID Family Member with Non-Sequence-Specific DNA Binding Activity

Peter B. Dallas,1,dagger Stephen Pacchione,1 Deborah Wilsker,1 Valerie Bowrin,1 Ryuji Kobayashi,2 and Elizabeth Moran1,*

Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140,1 and Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 117242

Received 10 January 2000/Returned for modification 31 January 2000/Accepted 3 February 2000

p270 is an integral member of human SWI-SNF complexes, first identified through its shared antigenic specificity with p300 and CREB binding protein. The deduced amino acid sequence of p270 reported here indicates that it is a member of an evolutionarily conserved family of proteins distinguished by the presence of a DNA binding motif termed ARID (AT-rich interactive domain). The ARID consensus and other structural features are common to both p270 and yeast SWI1, suggesting that p270 is a human counterpart of SWI1. The approximately 100-residue ARID sequence is present in a series of proteins strongly implicated in the regulation of cell growth, development, and tissue-specific gene expression. Although about a dozen ARID proteins can be identified from database searches, to date, only Bright (a regulator of B-cell-specific gene expression), dead ringer (a Drosophila melanogaster gene product required for normal development), and MRF-2 (which represses expression from the cytomegalovirus enhancer) have been analyzed directly in regard to their DNA binding properties. Each binds preferentially to AT-rich sites. In contrast, p270 shows no sequence preference in its DNA binding activity, thereby demonstrating that AT-rich binding is not an intrinsic property of ARID domains and that ARID family proteins may be involved in a wider range of DNA interactions.

* Corresponding author. Mailing address: Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA. Phone: (215) 707-7313. Fax: (215) 707-6989. E-mail: betty{at}unix.temple.edu.

dagger Present address: Institute for Child Health Research, University of Western Australia, West Perth, Western Australia, Australia.

Molecular and Cellular Biology, May 2000, p. 3137-3146, Vol. 20, No. 9
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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