Premium
Histone acetylation modulates the binding and remodeling activity of two different SWI/SNF complexes
Author(s) -
Chatterjee Nilanjana,
ShogrenKnaak Michael,
Bartholomew Blaine
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.lb195
Subject(s) - chromatin structure remodeling (rsc) complex , swi/snf , chromatin remodeling , bromodomain , nucleosome , acetylation , microbiology and biotechnology , histone , chromatin , chemistry , histone h4 , histone acetyltransferases , histone code , histone h3 , histone octamer , biochemistry , biology , dna , gene
The coordination of chromatin remodeling with chromatin modification is key to the regulation of chromatin structure and function. Recent studies implicated a functional link between histone acetylation and the SWI/SNF class of chromatin remodeling enzymes. This functional interplay is mediated via highly conserved acetyl‐lysine binding modules, the bromodomains. The presence of bromodomain (s) in SWI/SNF and RSC therefore strongly suggests that recognition of histone acetylation might play a major role in chromatin targeting and / or in their chromatin remodeling function. Here the nucleosome binding and remodeling activities of the two yeast SWI/SNF complexes were dissected out separately and the impact of histone tail acetylation on each of these processes was studied systematically. We show that histone H3 tail acetylation and not H4 augments nucleosome binding by actually enhancing the binding affinity of RSC and SWI/SNF complexes for nucleosomes. Further, H3 tail acetylation mediated enhanced binding of SWI/SNF mimics SWI/SNF recruitment by transcription activator Gal4‐VP16. Finally, kinetic analyses under saturating enzyme conditions revealed that rates of remodeling and ATP hydrolysis are both stimulated independent of nucleosome binding upon acetylation of H3 tails. Thus acetylation additionally modulates the catalytic activity of SWI/SNF complexes besides providing a unique recognition surface. This work was supported by Public Health Service grant GM 48413