Activation Domain–Mediated Targeting of the SWI/SNF Complex to Promoters Stimulates Transcription from Nucleosome Arrays

Neely, Kristen E.; Hassan, Ahmed H.E.; Wallberg, Annika E.; Steger, David J.; Cairns, Bradley R.; Wright, Anthony P. H.; Workman, Jerry L.

doi:10.1016/s1097-2765(00)80216-6

Cited by 234 publications

(233 citation statements)

References 52 publications

Supporting

Mentioning

215

Contrasting

Unclassified

Order By: Relevance

“…Results presented here indicate that the high levels of histone acetylation mediated by VP16, and its ability to recruit ATP-dependent chromatin remodeling complexes and histone acetyltransferases (65)(66)(67), are sufficient to fully abrogate the spreading of SIR complexes. In this assay, VP16 acts to increase histone acetylation on both sides of its binding site, thereby activating nearby genes irrespective of their location relative to the telomere, as expected from a local increase of HAT concentration.…”

Section: Discussionmentioning

confidence: 79%

Chromatin Domain Boundaries Delimited by a Histone-binding Protein in Yeast

Ferrari

Simmen

Dusserre

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

When located next to chromosomal elements such as telomeres, genes can be subjected to epigenetic silencing. In yeast, this is mediated by the propagation of the SIR proteins from telomeres toward more centromeric regions. Particular transcription factors can protect downstream genes from silencing when tethered between the gene and the telomere, and they may thus act as chromatin domain boundaries. Here we have studied one such transcription factor, CTF-1, that binds directly histone H3. A deletion mutagenesis localized the barrier activity to the CTF-1 histone-binding domain. A saturating point mutagenesis of this domain identified several amino acid substitutions that similarly inhibited the boundary and histone binding activities. Chromatin immunoprecipitation experiments indicated that the barrier protein efficiently prevents the spreading of SIR proteins, and that it separates domains of hypoacetylated and hyperacetylated histones. Together, these results suggest a mechanism by which proteins such as CTF-1 may interact directly with histone H3 to prevent the propagation of a silent chromatin structure, thereby defining boundaries of permissive and silent chromatin domains.The expression state of a eukaryotic gene depends in part on its location in the chromosome. This position effect results from the organization of eukaryotic genomes into discrete functional domains, defined by local differences in chromatin structure. The expression of genes within each domain appears to be defined and maintained by the concerted action of regulatory elements such as promoters, enhancers, silencers, and locus control regions. Individual domains may be bordered by boundary elements that separate regions of permissive and silent chromatin. Experimentally, boundary elements have been defined functionally by their ability to protect against position effect when flanking the assayed gene. Examples of boundary elements in metazoans include the subtelomeric anti-silencing regions at yeast telomeres, the scs and scsЈ elements flanking the 87A1 hsp70 locus in Drosophila, and the chicken ␤-globin boundary elements (1-4). Several proteins have been associated with barrier activities in yeast, Drosophila, and mammalian cells (5).Transcriptional repression of the yeast Saccharomyces cerevisiae subtelomeric regions is one of the best-studied examples of position-dependent gene expression. This phenomenon is referred to as telomere position effect and is similar to the position effect variegation (PEV) initially described in Drosophila (6). Transcriptional silencing at yeast telomeres is associated with a heterochromatin-like structure (7,8). DNA wrapped in transcriptionally silent chromatin replicates late in S phase and is refractory to some modifying agents. In addition, nucleosomes have reduced acetylation compared with nucleosomes from active region of the genome (9, 10).Transcriptional silencing at subtelomeric regions is mediated by a multiprotein nucleosome binding complex called the SIR complex, composed of the Sir2, Sir3, and...

show abstract

Section: Discussionmentioning

confidence: 79%

Chromatin Domain Boundaries Delimited by a Histone-binding Protein in Yeast

Ferrari

Simmen

Dusserre

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…This could occur through recruitment of chromatin-modifying complexes such as the SWI-SNF complex, or complexes capable of modifying histones, such as the GCN5-containing SAGA complex (14,26,45,55,56,65,72,83). The strong and general capability of artificially recruited GAL11 to activate transcription and to remodel the PHO5 promoter (18,21,22) suggests that such chromatin-modifying activity can be recruited along with the holoenzyme (76).…”

Section: Discussionmentioning

confidence: 99%

“…One possibility is that activators recruit any of various candidate chromatin remodeling complexes, which in turn alter local chromatin structure. This local remodeling could occur via histone acetylation following recruitment of GCN5 in the SAGA complex (72) or by alteration of histone-DNA interactions by the SWI-SNF complex, among other possibilities (14,45,55,56,65,83). In promoters that have a nucleosome positioned in close proximity to or incorporating the TATA element, such chromatin remodeling might be required to make the TATA element accessible to TFIID.…”

mentioning

confidence: 99%

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Ryan

Stafford

et al. 2000

Molecular and Cellular Biology

View full text Add to dashboard Cite

Transcriptional activators are believed to work in part by recruiting general transcription factors, such as TATA-binding protein (TBP) and the RNA polymerase II holoenzyme. Activation domains also contribute to remodeling of chromatin in vivo. To determine whether these two activities represent distinct functions of activation domains, we have examined transcriptional activation and chromatin remodeling accompanying artificial recruitment of TBP in yeast (Saccharomyces cerevisiae). We measured transcription of reporter genes with defined chromatin structure by artificial recruitment of TBP and found that a reporter gene whose TATA element was relatively accessible could be activated by artificially recruited TBP, whereas two promoters, GAL10 and CHA1, that have accessible activator binding sites, but nucleosomal TATA elements, could not. A third reporter gene containing the HIS4 promoter could be activated by GAL4-TBP only when a RAP1 binding site was present, although RAP1 alone could not activate the reporter, suggesting that RAP1 was needed to open the chromatin structure to allow activation. Consistent with this interpretation, artificially recruited TBP was unable to perturb nucleosome positioning via a nucleosomal binding site, in contrast to a true activator such as GAL4, or to perturb the TATA-containing nucleosome at the CHA1 promoter. Finally, we show that activation of the GAL10 promoter by GAL4, which requires chromatin remodeling, can occur even in swi gcn5 yeast, implying that remodeling pathways independent of GCN5, the SWI-SNF complex, and TFIID can operate during transcriptional activation in vivo.Transcriptional activators are thought to stimulate transcription of TATA-containing promoters in part by recruiting TFIID, a multiprotein complex consisting of the TATA-binding protein (TBP) and TBP-associated factors (TAFs), to the TATA box (25,60). Several in vitro and in vivo studies support this model. For example, transcription initiated at a mutated TATA element by induced synthesis of TBP with altered specificity was enhanced in both rate and extent in the presence of an activator that could bind upstream of the relevant promoter, consistent with activator-mediated recruitment (40). Recruitment has also been inferred from the results of "activator bypass" experiments in which artificial recruitment of TBP to promoter sites near the TATA element resulted in transcriptional activation, implying that TBP recruitment is a rate-limiting step in transcriptional activation in vivo (10,39,79). Most convincingly, chromatin immunoprecipitation experiments revealed TBP to be physically associated with promoters of numerous genes under activated, but not nonactivated, conditions, implying that recruitment accompanies activation (43,46).A potential obstacle to recruitment of TBP in vivo is posed by chromatin. Binding of TBP to nucleosomal TATA elements is greatly impeded in vitro (23, 32). Transcription is also strongly repressed by chromatin, but this repression can be largely alleviated by binding of act...

show abstract

Section: Transactivator-dependent Nucleosome Remodelling Complexes Anmentioning

confidence: 99%

“…Recent work indicates that genespeci®c activators target remodelling complexes to regulatory regions by directly interacting with them (Neely et al, 1999;Yudkovsky et al, 1999). These interactions are mediated by the activation domains of the transcription factors, which have been shown to recruit SNF/SWI remodelling activity to nucleosomal templates in vitro (Neely et al, 1999;Yudkovsky et al, 1999). Several authors have also reported the activatormediated targeting of chromatin remodelling complexes to transcriptional regulatory regions in vivo (Cosma et al, 1999;Fryer and Archer, 1998;KowenzLeutz and Leutz, 1999;Lee et al, 1999a).…”

Section: Transactivator-dependent Nucleosome Remodelling Complexes Anmentioning

confidence: 99%

Chromatin remodelling and DNA replication: from nucleosomes to loop domains

2001

View full text Add to dashboard Cite

Organization of DNA into chromatin is likely to participate in the control of the timing and selection of DNA replication origins. Reorganization of the chromatin is carried out by chromatin remodelling machines, which may a ect the choice of replication origins and e ciency of replication. Replication itself causes a profound rearrangement in the chromatin structure, from nucleosomes to DNA loop domains, allowing to retain or switch an epigenetic state. The present review considers the e ects of chromatin remodelling on replication and vice versa. Oncogene (2001) 20, 3086 ± 3093.

show abstract

Activation Domain–Mediated Targeting of the SWI/SNF Complex to Promoters Stimulates Transcription from Nucleosome Arrays

Cited by 234 publications

References 52 publications

Chromatin Domain Boundaries Delimited by a Histone-binding Protein in Yeast

Chromatin Domain Boundaries Delimited by a Histone-binding Protein in Yeast

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Chromatin remodelling and DNA replication: from nucleosomes to loop domains

Contact Info

Product

Resources

About