The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity

Dallas, P. B., Pacchione, S., Wilsker, D., Bowrin, V., Kobayashi, R., Moran, E. (May 2000) The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity. Molecular and Cellular Biology, 20 (9). pp. 3137-3146. ISSN 0270-7306

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URL: http://www.ncbi.nlm.nih.gov/pubmed/10757798
DOI: 10.1128/MCB.20.9.3137-3146.2000

Abstract

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.

Item Type: Paper
Uncontrolled Keywords: MAMMALIAN SWI/SNF COMPLEXES GLUCOCORTICOID RECEPTOR GENE TRANSCRIPTION REPRESSION ACTIVATION ENHANCER HOMOLOGY NUCLEOSOME REQUIRES
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor > CREB
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor > Cyclic AMP
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Kobayashi lab
Depositing User: Matt Covey
Date: May 2000
Date Deposited: 31 Jan 2014 14:50
Last Modified: 31 Jan 2014 14:50
PMCID: PMC85608
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29399

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