Swi/Snf dynamics on stress-responsive genes is governed by competitive bromodomain interactions

Cited 29 time in scopus
Metadata Downloads
Title
Swi/Snf dynamics on stress-responsive genes is governed by competitive bromodomain interactions
Author(s)
A Dutta; M Gogol; Jeong Hoon Kim; M Smolle; S Venkatesh; J Gilmore; L Florens; M P Washburn; J L Workman
Bibliographic Citation
Genes & Development, vol. 28, no. 20, pp. 2314-2330
Publication Year
2014
Abstract
The Swi/Snf chromatin remodeling complex functions to alter nucleosome positions by either sliding nucleosomes on DNA or the eviction of histones. The presence of histone acetylation and activator-dependent recruitment and retention of Swi/Snf is important for its efficient function. It is not understood, however, why such mechanisms are required to enhance Swi/Snf activity on nucleosomes. Snf2, the catalytic subunit of the Swi/Snf remodeling complex, has been shown to be a target of the Gcn5 acetyltransferase. Our study found that acetylation of Snf2 regulates both recruitment and release of Swi/Snf from stress-responsive genes. Also, the intramolecular interaction of the Snf2 bromodomain with the acetylated lysine residues on Snf2 negatively regulates binding and remodeling of acetylated nucleosomes by Swi/Snf. Interestingly, the presence of transcription activators mitigates the effects of the reduced affinity of acetylated Snf2 for acetylated nucleosomes. Supporting our in vitro results, we found that activator-bound genes regulating metabolic processes showed greater retention of the Swi/Snf complex even when Snf2 was acetylated. Our studies demonstrate that competing effects of (1) Swi/Snf retention by activators or high levels of histone acetylation and (2) Snf2 acetylation-mediated release regulate dynamics of Swi/Snf occupancy at target genes.
Keyword
ActivatorHistone acetylationStressSwi/Snf
ISSN
0890-9369
Publisher
Cold Spring Harbor Lab Press, Publications Dept
DOI
http://dx.doi.org/10.1101/gad.243584.114
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.