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

Kulesza, Caroline; Buskirk, Heather A. Van; Cole, Michael; Reese, Joseph C.; Smith, M. Mitchell; Engel, Daniel A.

doi:10.1038/sj.onc.1205201

Cited by 28 publications

(22 citation statements)

References 78 publications

(82 reference statements)

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“…Surprisingly, deletion of the AHC1 gene product, a unique structural subunit of the yeast ADA transcriptional activation complex, did not relieve the Gal4BD/IL-1NTP-mediated growth inhibition. These data suggested specific interference of Gal4BD/IL-1NTP with certain components of the yeast SAGA complex as it has been described for the acidic coactivators Gal4p, E1A, or VP16 (26,27,46). Similar results were obtained when identical yeast strains harboring the UAS GAL1 -TATA GAL1 -lacZ reporter and expressing Gal4BD, mouse Gal4BD/IL-1NTP, or the strong Gal4BD/ VP16 activator were assayed for their respective ␤-galactosidase activities (Fig.…”

Section: The Gal4bd/il-1ntp Fusion Protein Transactivates the Gal4 Prsupporting

confidence: 68%

“…The transcription factors containing the acidic-rich activation domain, such as yeast Gal4p, viral proteins VP16 and E1A, and human c-Jun and NF-B RelA(p65), are evolutionary well conserved, and are able to activate transcription in Saccharomyces cerevisiae as well as in mammalian cells (21)(22)(23)(24)(25). Moreover, the acidic transcription activators interact with different types of HATs and adaptor proteins, and their overexpression in yeast cells is often associated with growth inhibitory phenotypes (26,27).…”

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confidence: 99%

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Intracellular Interleukin-1α Functionally Interacts with Histone Acetyltransferase Complexes

Buryskova

Pospíšek

Grothey

et al. 2004

Journal of Biological Chemistry

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Interleukin-1␣ (IL-1␣) is an inflammatory cytokine acting extracellularly via membrane receptors. Interestingly, a significant portion of synthesized IL-1␣ is not secreted; instead, it is actively translocated into the cell nucleus. IL-1␣ was indeed shown to be involved in certain intracellular processes, such as control of proliferation, apoptosis, or migration, however, the mechanisms of such actions are not known. Here we show that intracellular IL-1␣ fused to the Gal4p DNA-binding domain (Gal4BD) possesses strong transactivation potential that can be boosted by overexpression of the transcriptional coactivator p300. We demonstrate that the IL-1␣ precursor interacts via its N-terminal peptide (IL-1NTP) with histone acetyltransferases p300, PCAF, Gcn5 and with the adaptor component Ada3, and that it integrates into the PCAF⅐p300 complex in a non-destructive manner. In analogy with known acidic coactivators, yeast strains expressing Gal4BD/IL-1NTP display a toxic phenotype that can be relieved by depletion of various components of the SAGA complex. Our data provide the first solid evidence for the nuclear target of the IL-1␣ precursor and suggest its novel function in transcriptional control.

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Section: The Gal4bd/il-1ntp Fusion Protein Transactivates the Gal4 Prsupporting

confidence: 68%

mentioning

confidence: 99%

Intracellular Interleukin-1α Functionally Interacts with Histone Acetyltransferase Complexes

Buryskova

Pospíšek

Grothey

et al. 2004

Journal of Biological Chemistry

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“…TRRAP interacts with c-Myc and E2F, oncogenic transcription factors frequently deregulated in human cancers, and this interaction is important for oncogenic transformation mediated by c-Myc and E2F . Similarly, the viral oncoprotein E1A targets TRRAP, an event that appears to be important for the transforming activity of E1A (Deleu et al, 2001;Kulesza et al, 2002). TRRAP is a binding partner of p53 and it may be important for posttranslational modification (acetylation) of the tumor suppressor Liu et al, 1999;Sykes et al, 2006;Tang et al, 2006) but also for the function of p53 on its target genes (Barlev et al, 2001;Ard et al, 2002).…”

Section: Possible Roles Of Trrap In Human Malignanciesmentioning

confidence: 99%

Orchestration of chromatin-based processes: mind the TRRAP

et al. 2007

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Chromatin modifications at core histones including acetylation, methylation, phosphorylation and ubiquitination play an important role in diverse biological processes. Acetylation of specific lysine residues within the N terminus tails of core histones is arguably the most studied histone modification; however, its precise roles in different cellular processes and how it is disrupted in human diseases remain poorly understood. In the last decade, a number of histone acetyltransferases (HATs) enzymes responsible for histone acetylation, has been identified and functional studies have begun to unravel their biological functions. The activity of many HATs is dependent on HAT complexes, the multiprotein assemblies that contain one HAT catalytic subunit, adapter proteins, several other molecules of unknown function and a large protein called TRansformation/tRanscription domain-Associated Protein (TRRAP). As a common component of many HAT complexes, TRRAP appears to be responsible for the recruitment of these complexes to chromatin during transcription, replication and DNA repair. Recent studies have shed new light on the role of TRRAP in HAT complexes as well as mechanisms by which it mediates diverse cellular processes. Thus, TRRAP appears to be responsible for a concerted and context-dependent recruitment of HATs and coordination of distinct chromatin-based processes, suggesting that its deregulation may contribute to diseases. In this review, we summarize recent developments in our understanding of the function of TRRAP and TRRAP-containing HAT complexes in normal cellular processes and speculate on the mechanism underlying abnormal events that may lead to human diseases such as cancer.

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“…To determine the role of Tra1 in Gal4-mediated transcriptional activation, we analyzed a tra1 temperaturesensitive mutant (Kulesza et al 2002). Figure 5B shows that inactivation of Tra1 substantially decreased transcription of GAL1 but not SED1, a SAGA-independent gene (Bhaumik and Green 2002).…”

Section: Genes and Development 335mentioning

confidence: 99%

“…Tra1 was C-terminally tagged with the myc epitope in the spt20⌬ strain FY1272 and its wild-type equivalent, FY251 (kindly provided by Fred Winston, Harvard Medical School) to generate TSGY30 and TSGY31, respectively. The tra1-ts (Kulesza et al 2002) and gal4⌬ (SGY14; Bhaumik and Green 2001) strains have been described.…”

Section: Yeast Strainsmentioning

confidence: 99%

In vivo target of a transcriptional activator revealed by fluorescence resonance energy transfer

Bhaumik¹,

Raha²,

Aiello³

et al. 2004

Genes Dev.

174

217

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Our understanding of eukaryotic transcriptional activation mechanisms has been hampered by an inability to identify the direct in vivo targets of activator proteins, primarily because of lack of appropriate experimental methods. To circumvent this problem, we have developed a fluorescence resonance energy transfer (FRET) assay to monitor interactions with transcriptional activation domains in living cells. We use this method to show that the Tra1 subunit of the SAGA (Spt/Ada/Gcn5/acetyltransferase) complex is the direct in vivo target of the yeast activator Gal4. Chromatin-immunoprecipitation experiments demonstrate that the Gal4-Tra1 interaction is required for recruitment of SAGA to the upstream activating sequence (UAS), and SAGA, in turn, recruits the Mediator complex to the UAS. The UAS-bound Mediator is required for recruitment of the general transcription factors to the core promoter. Thus, our results identify the in vivo target of an activator and show how the activator-target interaction leads to transcriptional stimulation. The FRET assay we describe is a general method that can be used to identify the in vivo targets of other activators. Transcription initiation by RNA polymerase II involves the assembly of general transcription factors (GTFs) on the core promoter to form a preinitiation complex (PIC). A variety of studies indicate that promoter-specific activator proteins (activators) work, at least in part, by increasing PIC formation (Orphanides et al. 1996;Roeder 1996;Ptashne and Gann 1997;. Activator-mediated stimulation of PIC assembly is believed to result from a direct interaction between the activation domain (AD) and one or more components of the transcription machinery, termed the "target." The unambiguous identification of the direct in vivo targets of activators has been a major challenge in the field.Transcriptional induction of genes involved in galactose utilization (GAL genes) has been a model experimental system for studying transcriptional activation mechanisms. The well-characterized acidic activator Gal4 is responsible for the transcriptional stimulation of GAL genes, such as GAL1, which contain Gal4-binding sites in their promoters (Johnston 1987;Johnston and Carlson 1992;Dudley et al. 1999). A variety of transcriptional components have been proposed to be the target of Gal4 including TBP (Melcher and Johnston 1995;Wu et al. 1996), TFIIB (Wu et al. 1996), Srb4 (Koh et al. 1998Park et al. 2000), Gal11 (Jeong et al. 2001), the Swi/Snf complex (Neely et al. 2002), and the SAGA (Spt/Ada/ Gcn5/acetyltransferase) complex (Bhaumik and Green 2001;Brown et al. 2001;Larschan and Winston 2001). These proposals are based on either in vitro protein interaction studies or inferences from various indirect in vivo experiments, and to date there is no definitive evidence that Gal4 directly interacts with any of these putative targets in vivo. The major obstacle has been the lack of an experimental strategy to measure direct interactions with transcriptional ADs in vivo.The development of spectra...

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

Cited by 28 publications

References 78 publications

Intracellular Interleukin-1α Functionally Interacts with Histone Acetyltransferase Complexes

Intracellular Interleukin-1α Functionally Interacts with Histone Acetyltransferase Complexes

Orchestration of chromatin-based processes: mind the TRRAP

In vivo target of a transcriptional activator revealed by fluorescence resonance energy transfer

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