Histone acetyltransferase complexes stabilize swi/snf binding to promoter nucleosomes.

Abstract:

:To investigate the function of SWI/SNF in site-specific chromatin remodeling at promoters, we have used a purified system to analyze its distribution, function, and retention following recruitment by a sequence-specific transcription activator. Activator recruitment of SWI/SNF bound the complex to promoter proximal nucleosomes and led to localized nucleosome disruption. However, retention of SWI/SNF on the promoter required either the continued binding of the transcription activator or acetylated histones. Histone acetylation by either the SAGA or NuA4 HAT complexes increased the retention of SWI/SNF on the promoter. These data illustrate a functional link between HAT complexes and the SWI/SNF chromatin remodeling complex and provide a mechanistic basis for the ordered recruitment of these complexes.

journal_name

Cell

journal_title

Cell

authors

Hassan AH,Neely KE,Workman JL

doi

10.1016/s0092-8674(01)00279-3

subject

Has Abstract

pub_date

2001-03-23 00:00:00

pages

817-27

issue

6

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(01)00279-3

journal_volume

104

pub_type

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