Eukaryotic Cell
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chandy, M.
Right arrow Articles by Workman, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chandy, M.
Right arrow Articles by Workman, J. L.

 Previous Article  |  Next Article 

Eukaryotic Cell, October 2006, p. 1738-1747, Vol. 5, No. 10
1535-9778/06/$08.00+0     doi:10.1128/EC.00165-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SWI/SNF Displaces SAGA-Acetylated Nucleosomes

Mark Chandy,1,2 José L. Gutiérrez,1 Philippe Prochasson,1 and Jerry L. Workman1*

Stowers Institute for Medical Research, 1000 E 50th St., Kansas City, Missouri 64110,1 Penn State University College of Medicine, 500 University St., Hershey, Pennsylvania 170332

Received 5 June 2006/ Accepted 5 July 2006

SWI/SNF is a well-characterized chromatin remodeling complex that remodels chromatin by sliding nucleosomes in cis and/or displacing nucleosomes in trans. The latter mechanism has the potential to remove promoter nucleosomes, allowing access to transcription factors and RNA polymerase. In vivo, histone acetylation often precedes apparent nucleosome loss; therefore, we sought to determine whether nucleosomes containing acetylated histones could be displaced by the SWI/SNF chromatin remodeling complex. We found that SAGA-acetylated histones were lost from an immobilized nucleosome array when treated with the SWI/SNF complex. When the nucleosome array was acetylated by SAGA in the presence of bound transcription activators, it generated a peak of acetylation surrounding the activator binding sites. Subsequent SWI/SNF treatment suppressed this acetylation peak. Immunoblots indicated that SWI/SNF preferentially displaced acetylated histones from the array relative to total histones. Moreover, the Swi2/Snf2 bromodomain, an acetyl-lysine binding domain, played a role in the displacement of acetylated histones. These data indicate that targeted histone acetylation by the SAGA complex predisposes promoter nucleosomes for displacement by the SWI/SNF complex.

* Corresponding author. Mailing address: Stowers Institute for Medical Research, 1000 E 50th St., Kansas City, MO 64110. Phone: (816) 926-4310. Fax: (816) 926-4686. E-mail: jlw{at}stowers-institute.org.

Eukaryotic Cell, October 2006, p. 1738-1747, Vol. 5, No. 10
1535-9778/06/$08.00+0     doi:10.1128/EC.00165-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Appl. Environ. Microbiol. Infect. Immun. J. Bacteriol.
Mol. Cell Biol. Microbiol. Mol. Biol. Rev. ALL ASM JOURNALS
Copyright © 2006 by the American Society for Microbiology.