Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc

Kurabe, Nobuya; Katagiri, Kumiko; Komiya, Yuko; Ito, Rie; Sugiyama, Akinori; Kawasaki, Yasushi; Tashiro, Fumio

doi:10.1038/sj.onc.1210349

Cited by 34 publications

(50 citation statements)

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“…The ySAGA complex shares a high degree of similarity with the human TFTC/STAGA/PCAF complexes in subunit content, structure, and function (references 34 and 52 and references therein). The exact composition of the human complexes is still not known; however, recently, several new mammalian homologues of ySAGA subunits have been described (25,57,59). These reports further demonstrate that the ySAGA and human TFTC/STAGA/PCAF complexes are functionally and structurally equivalent entities and that a SAGA-type complex can be purified from species all along the evolutionary scale (34).…”

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confidence: 75%

The Human SPT20-Containing SAGA Complex Plays a Direct Role in the Regulation of Endoplasmic Reticulum Stress-Induced Genes

Nagy

Riss

Romier

et al. 2009

Molecular and Cellular Biology

101

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One of the central questions in eukaryotic transcription is how activators can transmit their signal to stimulate gene expression in the context of chromatin. The multisubunit SAGA coactivator complex has both histone acetyltransferase and deubiquitination activities and remodels chromatin to allow transcription. Whether and how SAGA is able to regulate transcription at specific loci is poorly understood. Using mass spectrometry, immunoprecipitation, and Western blot analysis, we have identified human SPT20 (hSPT20) as the human homologue of the yeast Spt20 and show that hSPT20 is a bona fide subunit of the human SAGA (hSAGA; previously called TFTC/STAGA/PCAF) complex and that hSPT20 is required for the integrity of the hSAGA complex. We demonstrate that hSPT20 and other hSAGA subunits, together with RNA polymerase II, are specifically recruited to genes induced by endoplasmic reticulum (ER) stress. In good agreement with the recruitment of hSAGA to the ER stress-regulated genes, knockdown of hSTP20 hampers ER stress response. Surprisingly, hSPT20 recruitment was not observed for genes induced by another type of stress. These results provide evidence for a direct and specific role of the hSPT20-containing SAGA complex in transcriptional induction of ER stress-responsive genes. Thus, hSAGA regulates the transcription of stress-responsive genes in a stress type-dependent manner.The ordered assembly of a functional preinitiation complex is a prerequisite for the transcription of RNA polymerase II (Pol II). Besides the general transcription factors, the presence of transcriptional activators and cofactors is necessary to make the transcription initiation a tightly regulated process. In addition, activators and repressors have to communicate with the promoter-bound factors in the context of chromatin. To achieve this, chromatin has to be opened, a process which is carried out by ATP-dependent chromatin remodelers and promoted by enzymes catalyzing posttranslational modifications of histone tails (23,40

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mentioning

confidence: 75%

The Human SPT20-Containing SAGA Complex Plays a Direct Role in the Regulation of Endoplasmic Reticulum Stress-Induced Genes

Nagy

Riss

Romier

et al. 2009

Molecular and Cellular Biology

101

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“…Although studies in vivo have connected the presence of H3K4me3 to transcriptional activation by the SAGA complex (30,31,46), the way by which SAGA transduces H3K4me3 recognition into hyperacetylation by Gcn5 was not known. In this study we uncover a mechanism by which the HAT subcomplex of the SAGA transcriptional coactivator couples histone hyperacetylation to H3K4 trimethylation, a universal mark associated with promoter regions of actively transcribed chromatin in organisms ranging from yeast (9,47) to humans (48).…”

Section: Discussionmentioning

confidence: 99%

Nucleosome competition reveals processive acetylation by the SAGA HAT module

Ringel

Cieniewicz

Taverna

et al. 2015

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

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The Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator complex hyperacetylates histone tails in vivo in a manner that depends upon histone 3 lysine 4 trimethylation (H3K4me3), a histone mark enriched at promoters of actively transcribed genes. SAGA contains a separable subcomplex known as the histone acetyltransferase (HAT) module that contains the HAT, Gcn5, bound to Sgf29, Ada2, and Ada3. Sgf29 contains a tandem Tudor domain that recognizes H3K4me3-containing peptides and is required for histone hyperacetylation in vivo. However, the mechanism by which H3K4me3 recognition leads to lysine hyperacetylation is unknown, as in vitro studies show no effect of the H3K4me3 modification on histone peptide acetylation by Gcn5. To determine how H3K4me3 binding by Sgf29 leads to histone hyperacetylation by Gcn5, we used differential fluorescent labeling of histones to monitor acetylation of individual subpopulations of methylated and unmodified nucleosomes in a mixture. We find that the SAGA HAT module preferentially acetylates H3K4me3 nucleosomes in a mixture containing excess unmodified nucleosomes and that this effect requires the Tudor domain of Sgf29. The H3K4me3 mark promotes processive, multisite acetylation of histone H3 by Gcn5 that can account for the different acetylation patterns established by SAGA at promoters versus coding regions. Our results establish a model for Sgf29 function at gene promoters and define a mechanism governing crosstalk between histone modifications.T he different patterns of histone posttranslational modifications distributed across the genome are proposed to constitute a "histone code" that orchestrates distinct transcriptional programs by recruiting specific effector proteins (1-4). The phenomenon of histone code "crosstalk," whereby one type of histone modification directs the establishment of another, or through which several histone modifications are recognized in tandem, has emerged as an important and widespread mechanism regulating chromatin-templated processes (5, 6). The multifunctional complexes that activate transcription are thought to mediate crosstalk through "reader" domains that recognize particular chromatin marks as well as through catalytic subunits that deposit or remove histone modifications (5,7,8). As a result, distinct combinations of histone posttranslational modifications that correlate with transcriptional output cluster across the genome (9-11). High levels of histone 3 lysine 4 trimethylation (H3K4me3) and histone H3 hyperacetylation are present at the promoters of actively transcribed genes (9,11,12), and multiple lines of evidence support the existence of regulatory mechanisms coupling the two modifications. Studies using tandem mass spectrometry to sequence whole histone tails have shown that H3K4me3 is highly correlated with hyperacetylation of the same H3 tail (13,14). Deleting the yeast Set1 methyltransferase, which trimethylates H3K4, leads to dramatically lower levels of histone H3 tail acetylation overall (13, 15). These results are consistent with ...

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“…A novel proteomic investigation of the yeast SAGA complex has identified three novel SAGA-associated factors (Sgf73, Sgf29 and Sgf11) together with Ubp8, a ubiquitin-specific protease component, which suggested that a second enzymatic activity exists within these complexes (Sanders et al, 2002;Powell et al, 2004). Recently, it became clear that the vertebrate homologues of some of the novel yeast SAGA factors (ATXN7 and SGF29 in Table 1) are also present in either STAGA or TFTC (Helmlinger et al, 2004;Palhan et al, 2005;Kurabe et al, 2007). While the originally described human TFTC, PCAF/GCN5 and STAGA complexes shared a number of common subunits, they did not seem to be identical, suggesting variations due to their distinct purification protocols or the existence of functional difference between these complexes.…”

Section: Introductionmentioning

confidence: 99%

“…Concerning the PCAF complex, further analysis will be necessary to compare this complex to the STAGA/ TFTC complexes. The identification of hADA2a as a subunit of the PCAF complex would make this complex different from STAGA and TFTC complexes, in which ADA2a is not present, The factors, described in the different complexes (Grant et al, 1997(Grant et al, , 1998aMartinez et al, 1998Martinez et al, , 2001Wieczorek et al, 1998;Brand et al, 1999b;Eberharter et al, 1999;Georgieva et al, 2001;Kusch et al, 2003;Muratoglu et al, 2003;Helmlinger et al, 2004;Rodriguez-Navarro et al, 2004;Palhan et al, 2005;Guelman et al, 2006a;Demeny et al, 2007;Kurabe et al, 2007), are represented on a horizontal line as homologues from different species. Different names on a horizontal line mean that these homologues are known under different names in different species.…”

Section: Introductionmentioning

confidence: 99%

Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation

2007

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Transcription in eukaryotes is a tightly regulated, multistep process. Gene-specific transcriptional activators, several different co-activators and general transcription factors are necessary to access specific loci to allow precise initiation of RNA polymerase II transcription. As the dense chromatin folding of the genome does not allow the access of these sites by the huge multiprotein transcription machinery, remodelling is required to loosen up the chromatin structure for successful transcription initiation. In the present review, we summarize the recent evolution of our understanding of the function of two histone acetyl transferases (ATs) from metazoan organisms: GCN5 and PCAF. Their overall structure and the multiprotein complexes in which they are carrying out their activities are discussed. Metazoan GCN5 and PCAF are subunits of at least two types of multiprotein complexes, one having a molecular weight of 2 MDa (SPT3-TAF9-GCN5 acetyl transferase/TATA binding protein (TBP)-free-TAF complex/PCAF complexes) and a second type with about a size of 700 kDa (ATAC complex). These complexes possess global histone acetylation activity and locus-specific co-activator functions together with AT activity on non-histone substrates. Thus, their biological functions cover a wide range of tasks and render them indispensable for the normal function of cells. That deregulation of the global and/or specific AT activities of these complexes leads to the cancerous transformation of the cells highlights their importance in cellular processes. The possible effects of GCN5 and PCAF in tumorigenesis are also discussed.

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Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc

Cited by 34 publications

References 25 publications

The Human SPT20-Containing SAGA Complex Plays a Direct Role in the Regulation of Endoplasmic Reticulum Stress-Induced Genes

The Human SPT20-Containing SAGA Complex Plays a Direct Role in the Regulation of Endoplasmic Reticulum Stress-Induced Genes

Nucleosome competition reveals processive acetylation by the SAGA HAT module

Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation

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