Histone Acetyltransferase Complexes Stabilize SWI/SNF Binding to Promoter Nucleosomes

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

doi:10.1016/s0092-8674(01)00279-3

Cited by 332 publications

(249 citation statements)

References 56 publications

(2 reference statements)

Supporting

Mentioning

229

Contrasting

Unclassified

Order By: Relevance

“…Also shown are anti-GST Western blots of the whole cell lysates used for immunoprecipitation between components of SAGA and SWI/SNF, suggesting a functional relationship between these complexes (Pollard and Peterson, 1997;Roberts and Winston, 1997;Sterner et al, 1999). It has also been shown that acetylation of the N-terminal tails of histones can modify SWI/SNF function and processivity (Logie et al, 1999), and additional genetic and biochemical interactions between SAGA and SWI/ SNF have been reported (Cosma et al, 1999;Hassan et al, 2001;Krebs et al, 2000;Syntichaki et al, 2000). If E1A were acting here simply to ablate SAGA or SWI/SNF function, then the reported synthetic lethality observed in double mutants of SWI/SNF and SAGA would lead to the prediction that expression of E1A in cells containing single mutations that disrupt either complex, would cause death.…”

Section: Discussionmentioning

confidence: 98%

Adenovirus E1A requires the yeast SAGA histone acetyltransferase complex and associates with SAGA components Gcn5 and Tra1

et al. 2002

View full text Add to dashboard Cite

The budding yeast Saccharomyces cerevisiae was used as a model system to study the function of the adenovirus E1A oncoprotein. Previously we demonstrated that expression of the N-terminal 82 amino acids of E1A in yeast causes pronounced growth inhibition and speci®cally interferes with SWI/SNF-dependent transcriptional activation. Further genetic analysis identi®ed the yeast transcription factor Adr1 as a high copy suppressor of E1A function. Transcriptional activation by Adr1 requires interaction with co-activator proteins Ada2 and Gcn5, components of histone acetyltransferase complexes including ADA and SAGA. Analysis of mutant alleles revealed that several components of the SAGA complex, including proteins from the Ada, Spt, and Taf classes were required for E1A-induced growth inhibition. Growth inhibition also depended on the Gcn5 histone acetyltransferase, and point mutations within the Gcn5 HAT domain rendered cells E1A-resistant. Also required was SAGA component Tra1, a homologue of the mammalian TRRAP protein which is required for c-myc and E1A induced cellular transformation. Additionally, Gcn5 protein could associate with E1A in vitro in a manner that depended on the N-terminal domain of E1A, and Tra1 protein was coimmunoprecipitated with E1A in vivo. These results indicate a strong requirement for intact SAGA complex for E1A to function in yeast, and suggest a role for SAGA-like complexes in mammalian cell transformation.

show abstract

Section: Discussionmentioning

confidence: 98%

Adenovirus E1A requires the yeast SAGA histone acetyltransferase complex and associates with SAGA components Gcn5 and Tra1

et al. 2002

View full text Add to dashboard Cite

show abstract

“…Whereas Clr3 preferentially targets histone H3 lysine 14, Clr6 displays broad substrate specificity for lysine residues on both histone H3 and H4 tails (50). Deacetylation of histones by these activities may prevent binding of factors such as SWI/SNF that remodel chromatin to provide access to the transcriptional machinery (51). Alternatively, HP1-associated Clr6 and SHREC complexes might act together to remove acetyl groups from histones, and to facilitate the proper positioning of nucleosomes required for higher-order chromatin assembly (22,23,52).…”

Section: Discussionmentioning

confidence: 99%

Diverse roles of HP1 proteins in heterochromatin assembly and functions in fission yeast

Fischer

Cui

Dhakshnamoorthy

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

137

175

View full text Add to dashboard Cite

“…Histone modifications were however found to effect the interaction of SWI/SNF with nucleosomes. Acetylation by SAGA and NuA4 was found to stabilize SWI/ SNF interaction with nucleosome in a bromodomain dependent manner [49,145]. Acetylation of lysine 8 of histone H4 has also been shown to facilitate recruitment of SWI/SNF [146].…”

Section: Role Of Histone Tails and Their Modification In Chromatin Rementioning

confidence: 97%

Mechanisms of ATP dependent chromatin remodeling

Gangaraju

Bartholomew

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

128

159

View full text Add to dashboard Cite

The inter-relationship between DNA repair and ATP dependent chromatin remodeling has begun to become very apparent with recent discoveries. ATP dependent remodeling complexes mobilize nucleosomes along DNA, promote the exchange of histones, or completely displace nucleosomes from DNA. These remodeling complexes are often categorized based on the domain organization of their catalytic subunit. The biochemical properties and structural information of several of these remodeling complexes are reviewed. The different models for how these complexes are able to mobilize nucleosomes and alter nucleosome structure are presented incorporating several recent findings. Finally the role of histone tails and their respective modifications in ATP-dependent remodeling are discussed.

show abstract

Histone Acetyltransferase Complexes Stabilize SWI/SNF Binding to Promoter Nucleosomes

Cited by 332 publications

References 56 publications

Adenovirus E1A requires the yeast SAGA histone acetyltransferase complex and associates with SAGA components Gcn5 and Tra1

Adenovirus E1A requires the yeast SAGA histone acetyltransferase complex and associates with SAGA components Gcn5 and Tra1

Diverse roles of HP1 proteins in heterochromatin assembly and functions in fission yeast

Mechanisms of ATP dependent chromatin remodeling

Contact Info

Product

Resources

About