Host Cell Factor and an Uncharacterized SANT Domain Protein Are Stable Components of ATAC, a Novel dAda2A/dGcn5-Containing Histone Acetyltransferase Complex in <i>Drosophila</i>

Guelman, Sebastián; Suganuma, Tamaki; Florens, Laurence; Swanson, Selene K.; Kiesecker, Cheri L.; Kusch, T; Anderson, Scott; Yates, John R.; Washburn, Michael P.; Abmayr, Susan M.; Workman, Jerry L.

doi:10.1128/mcb.26.3.871-882.2006

Cited by 109 publications

(135 citation statements)

References 50 publications

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“…A few other proteins were also recovered but are likely nonspecific, as all corresponded to highly abundant ribosomal proteins, translation factors, and metabolic enzymes. We did not detect additional subunits that have been identified as part of related SAGA complexes, such as Chd1, Rtg2, and Ahc1 in S. cerevisiae, or Atac1 in Drosophila melanogaster Pray-Grant et al 2002Guelman et al 2006). BLAST searches failed to identify proteins orthologous to S. cerevisiae Rtg2 and Ahc1 or to D. melanogaster Atac1 in S. pombe.…”

Section: Resultsmentioning

confidence: 76%

The S. pombe SAGA complex controls the switch from proliferation to sexual differentiation through the opposing roles of its subunits Gcn5 and Spt8

Helmlinger¹,

Marguerat²,

Villén³

et al. 2008

Genes Dev.

122

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The SAGA complex is a conserved multifunctional coactivator known to play broad roles in eukaryotic transcription. To gain new insights into its functions, we performed biochemical and genetic analyses of SAGA in the fission yeast, Schizosaccharomyces pombe. Purification of the S. pombe SAGA complex showed that its subunit composition is identical to that of Saccharomyces cerevisiae. Analysis of S. pombe SAGA mutants revealed that SAGA has two opposing roles regulating sexual differentiation. First, in nutrient-rich conditions, the SAGA histone acetyltransferase Gcn5 represses ste11 + , which encodes the master regulator of the mating pathway. In contrast, the SAGA subunit Spt8 is required for the induction of ste11 + upon nutrient starvation. Chromatin immunoprecipitation experiments suggest that these regulatory effects are direct, as SAGA is physically associated with the ste11 + promoter independent of nutrient levels. Genetic tests suggest that nutrient levels do cause a switch in SAGA function, as spt8⌬ suppresses gcn5⌬ with respect to ste11 + derepression in rich medium, whereas the opposite relationship, gcn5⌬ suppression of spt8⌬, occurs during starvation. Thus, SAGA plays distinct roles in the control of the switch from proliferation to differentiation in S. pombe through the dynamic and opposing activities of Gcn5 and Spt8.[Keywords: S. pombe; transcription; differentiation; SAGA; Gcn5; Ste11] Supplemental material is available at http://www.genesdev.org.

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Section: Resultsmentioning

confidence: 76%

The S. pombe SAGA complex controls the switch from proliferation to sexual differentiation through the opposing roles of its subunits Gcn5 and Spt8

Helmlinger¹,

Marguerat²,

Villén³

et al. 2008

Genes Dev.

122

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“…SAGA contains about 18‐20 subunits, which are organized in histone acetyltransferase (HAT), histone H2Bub1 deubiquitinase (DUB) and TATA binding protein (TBP) regulatory and structural modules (Lee et al , 2011; Spedale et al , 2012). Metazoan GCN5 was also identified as a subunit of a second coactivator HAT complex in Drosophila and mammals, named ATAC (Ada Two A Containing; Guelman et al , 2006; Wang et al , 2008; Nagy et al , 2010). ATAC contains 10 well‐characterized subunits.…”

Section: Introductionmentioning

confidence: 99%

Coactivators and general transcription factors have two distinct dynamic populations dependent on transcription

et al. 2017

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SAGA and ATAC are two distinct chromatin modifying co‐activator complexes with distinct enzymatic activities involved in RNA polymerase II (Pol II) transcription regulation. To investigate the mobility of co‐activator complexes and general transcription factors in live‐cell nuclei, we performed imaging experiments based on photobleaching. SAGA and ATAC, but also two general transcription factors (TFIID and TFIIB), were highly dynamic, exhibiting mainly transient associations with chromatin, contrary to Pol II, which formed more stable chromatin interactions. Fluorescence correlation spectroscopy analyses revealed that the mobile pool of the two co‐activators, as well as that of TFIID and TFIIB, can be subdivided into “fast” (free) and “slow” (chromatin‐interacting) populations. Inhibiting transcription elongation decreased H3K4 trimethylation and reduced the “slow” population of SAGA, ATAC, TFIIB and TFIID. In addition, inhibiting histone H3K4 trimethylation also reduced the “slow” populations of SAGA and ATAC. Thus, our results demonstrate that in the nuclei of live cells the equilibrium between fast and slow population of SAGA or ATAC complexes is regulated by active transcription via changes in the abundance of H3K4me3 on chromatin.

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“…More recently, HCF-1 has been shown to be a component of multiple chromatin modification complexes that contain histone methyltransferase (Set1, MLL family members) (2-4), demethylase (LSD1) (5), acetyltransferase (ATAC/STAGA, MOF) (6)(7)(8), and deacetylase (sin3a/HDAC) (2) activities. Thus, HCF-1 functions to bridge transcription factors and chromatin modulation machinery.…”

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confidence: 99%

Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components

Peng

Nogueira

Vogel

et al. 2010

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

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The cellular transcriptional coactivator HCF-1 interacts with numerous transcription factors as well as other coactivators and is a component of multiple chromatin modulation complexes. The protein is essential for the expression of the immediate early genes of both herpes simplex virus (HSV) and varicella zoster virus and functions, in part, by coupling chromatin modification components including the Set1 or MLL1 histone methyltransferases and the histone demethylase LSD1 to promote the installation of positive chromatin marks and the activation of viral immediately early gene transcription. Although studies have investigated the role of HCF-1 in both cellular and viral transcription, little is known about other processes that the protein may be involved in. Here we demonstrate that HCF-1 localizes to sites of HSV replication late in infection. HCF-1 interacts directly and simultaneously with both HSV DNA replication proteins and the cellular histone chaperone Asf1b, a protein that regulates the progression of cellular DNA replication forks via chromatin reorganization. Asf1b localizes with HCF-1 in viral replication foci and depletion of Asf1b results in significantly reduced viral DNA accumulation. The results support a model in which the transcriptional coactivator HCF-1 is a component of the HSV DNA replication assembly and promotes viral DNA replication by coupling Asf1b to DNA replication components. This coupling provides a novel function for HCF-1 and insights into the mechanisms of modulating chromatin during DNA replication.

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Host Cell Factor and an Uncharacterized SANT Domain Protein Are Stable Components of ATAC, a Novel dAda2A/dGcn5-Containing Histone Acetyltransferase Complex in Drosophila

Cited by 109 publications

References 50 publications

The S. pombe SAGA complex controls the switch from proliferation to sexual differentiation through the opposing roles of its subunits Gcn5 and Spt8

The S. pombe SAGA complex controls the switch from proliferation to sexual differentiation through the opposing roles of its subunits Gcn5 and Spt8

Coactivators and general transcription factors have two distinct dynamic populations dependent on transcription

Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components

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