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

P. B. Dallas, S. Pacchione, D. Wilsker, V. Bowrin, R. Kobayashi, E. Moran

Research output: Contribution to journalArticlepeer-review

96 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)3137-3146
Number of pages10
JournalMolecular and cellular biology
Volume20
Issue number9
DOIs
StatePublished - 2000

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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