Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (314K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (12)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Wilsker, D.
Right arrow Articles by Moran, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wilsker, D.
Right arrow Articles by Moran, E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 24 February 2004

Nucleic Acids Research, 2004, Vol. 32, No. 4 1345-1353
© 2004 Oxford University Press

The DNA-binding properties of the ARID-containing subunits of yeast and mammalian SWI/SNF complexes

Deborah Wilsker, Antonia Patsialou, Steven D. Zumbrun, Suhkmann Kim1, Yuan Chen1, Peter B. Dallas2 and Elizabeth Moran*

Fels Institute for Cancer Research, Temple University School of Medicine, Philadelphia, PA, USA 1 Beckman Research Institute of the City of Hope, Duarte, CA, USA and 2 TVW Telethon Institute for Child Health Research and the Center for Child Health Research, Subiaco, Australia

*To whom correspondence should be addressed. Tel: +1 215 707 7313; Fax: +1 215 707 6989; Email: betty{at}temple.edu

SWI/SNF complexes are ATP-dependent chromatin remodeling complexes that are highly conserved from yeast to human. From yeast to human the complexes contain a subunit with an ARID (A-T-rich interaction domain) DNA-binding domain. In yeast this subunit is SWI1 and in human there are two closely related alternative subunits, p270 and ARID1B. We describe here a comparison of the DNA-binding properties of the yeast and human SWI/SNF ARID-containing subunits. We have determined that SWI1 is an unusual member of the ARID family in both its ARID sequence and in the fact that its DNA-binding affinity is weaker than that of other ARID family members, including its human counterparts, p270 and ARID1B. Sequence analysis and substitution mutagenesis reveals that the weak DNA-binding affinity of the SWI1 ARID is an intrinsic feature of its sequence, arising from specific variations in the major groove interaction site. In addition, this work confirms the finding that p270 binds DNA without regard to sequence specificity, excluding the possibility that the intrinsic role of the ARID is to recruit SWI/SNF complexes to specific promoter sequences. These results emphasize that care must be taken when comparing yeast and higher eukaryotic SWI/SNF complexes in terms of DNA-binding mechanisms.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
K. W. Trotter, H.-Y. Fan, M. L. Ivey, R. E. Kingston, and T. K. Archer
The HSA Domain of BRG1 Mediates Critical Interactions Required for Glucocorticoid Receptor-Dependent Transcriptional Activation In Vivo
Mol. Cell. Biol., February 15, 2008; 28(4): 1413 - 1426.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Huarte, F. Lan, T. Kim, M. W. Vaughn, M. Zaratiegui, R. A. Martienssen, S. Buratowski, and Y. Shi
The Fission Yeast Jmj2 Reverses Histone H3 Lysine 4 Trimethylation
J. Biol. Chem., July 27, 2007; 282(30): 21662 - 21670.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Kim, L. Probst, C. Das, and P. W. Tucker
REKLES Is an ARID3-restricted Multifunctional Domain
J. Biol. Chem., May 25, 2007; 282(21): 15768 - 15777.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C.-H. Wang, L.-H. Su, and C.-H. Sun
A Novel ARID/Bright-like Protein Involved in Transcriptional Activation of Cyst Wall Protein 1 Gene in Giardia lamblia
J. Biol. Chem., March 23, 2007; 282(12): 8905 - 8914.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
A. Patsialou, D. Wilsker, and E. Moran
DNA-binding properties of ARID family proteins
Nucleic Acids Res., January 7, 2005; 33(1): 66 - 80.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.