Histone acetyltransferase complexes stabilize SWI/SNF binding to promoter nucleosomes

Ahmed H. Hassan; Kristen E. Neely; Jerry L. Workman

doi:10.1016/S0092-8674(01)00279-3

Histone acetyltransferase complexes stabilize SWI/SNF binding to promoter nucleosomes

Ahmed H. Hassan, Kristen E. Neely, Jerry L. Workman

Research output: Contribution to journal › Article › peer-review

303 Citations (Scopus)

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.

Original language	English
Pages (from-to)	817-827
Number of pages	11
Journal	Cell
Volume	104
Issue number	6
DOIs	https://doi.org/10.1016/S0092-8674(01)00279-3
Publication status	Published - Mar 23 2001
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/S0092-8674(01)00279-3

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title = "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.",

author = "Hassan, {Ahmed H.} and Neely, {Kristen E.} and Workman, {Jerry L.}",

note = "Funding Information: We thank L. Howe for advice in designing experiments and M. Vignali for assistance in quantifying data and editing this manuscript. We thank C. Peterson for suggesting the experiment shown in Figure 5 . We are grateful to B. Cairns for providing α Swp61/Arp7 and other antibodies against SWI/SNF subunits. We thank M. Carey for the pG5E4T plasmid, and K. Ikeda for pG5E4-5S. We also thank F. Pugh for a Gal4-proline expression plasmid and R. Utley for Gal4-VP16 purification. We are grateful to J. Cote, T. Owen-Hughes, A. Eberharter, and members of the Workman, Simpson, and Reese labs at Penn State University for many helpful comments during this study. This work was supported by a grant from NIGMS (to J. L. W.). J. L. W. is an Associate Investigator with the Howard Hughes Medical Institute.",

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AU - Hassan, Ahmed H.

AU - Neely, Kristen E.

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N1 - Funding Information: We thank L. Howe for advice in designing experiments and M. Vignali for assistance in quantifying data and editing this manuscript. We thank C. Peterson for suggesting the experiment shown in Figure 5 . We are grateful to B. Cairns for providing α Swp61/Arp7 and other antibodies against SWI/SNF subunits. We thank M. Carey for the pG5E4T plasmid, and K. Ikeda for pG5E4-5S. We also thank F. Pugh for a Gal4-proline expression plasmid and R. Utley for Gal4-VP16 purification. We are grateful to J. Cote, T. Owen-Hughes, A. Eberharter, and members of the Workman, Simpson, and Reese labs at Penn State University for many helpful comments during this study. This work was supported by a grant from NIGMS (to J. L. W.). J. L. W. is an Associate Investigator with the Howard Hughes Medical Institute.

PY - 2001/3/23

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N2 - 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.

AB - 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.

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Histone acetyltransferase complexes stabilize SWI/SNF binding to promoter nucleosomes

Abstract

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