The embryonic transcription factor stage specific activator protein contains a potent bipartite activation domain that interacts with several RNA polymerase II basal transcription factors.

Defalco, Jeffery; Childs, Geoffrey

doi:10.1073/pnas.93.12.5802

Cited by 12 publications

(22 citation statements)

References 35 publications

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“…TFIID reconstitution experiments indicate that TAF110 is required for the response to Sp1; a combination of TBP, TAF250 and TAF110 confers a modest activation by Sp1, and the addition of TAF150 confers robust Sp1-dependent activation (Chen et al 1994). TAF110 also interacts with a variety of other activators (Schulman et al 1995;DeFalco & Childs 1996;Lala et al 1996;Coustry et al 1998). Interestingly, S. cerevisiae does not contain a homologue of TAF110, although it contains homologues for all other TAFs found in¯ies and mammals (Moqtaderi et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Incorporation of Drosophila TAF110 into the yeast TFIID complex does not permit the Sp1 glutamine‐rich activation domain to function in vivo

Keaveney

Struhl

1999

Genes to Cells

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Background: Acidic activation domains function across eukaryotic species, and hence stimulate transcription by a conserved molecular mechanism. In contrast, glutamine-rich activation domains function in¯ies, mammals, and ®ssion yeasts but not in the budding yeast Saccharomyces cerevisiae. The glutamine-rich activation domain of Sp1 interacts with TAF110, and it has been suggested that this interaction is important for transcriptional activation. S. cerevisiae does not contain a homologue of TAF110, suggesting a potential mechanism to account for the failure of glutamine-rich activation domains to stimulate transcription.

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Section: Introductionmentioning

confidence: 99%

Incorporation of Drosophila TAF110 into the yeast TFIID complex does not permit the Sp1 glutamine‐rich activation domain to function in vivo

Keaveney

Struhl

1999

Genes to Cells

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“…As a result, they are classified mainly by the relative abundance of particular amino acids in the peptide that supports activation (8). Such classes of activation regions include those rich in glutamine (69), glutamine/glycine (32), proline (2, 4), isoleucine (5), leucine (37), serine/threonine (24,32), and acidic (6,7,25,38,58,70) amino acids. These regions reportedly range in size from compact (23 amino acids in the case of p53) to the full length of the activator protein (50,67).…”

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confidence: 99%

The minimal transactivation region of Saccharomyces cerevisiae Gln3p is localized to 13 amino acids

Svetlov

Cooper

1997

J Bacteriol

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Regulated nitrogen catabolic gene transcription in Saccharomyces cerevisiae is mediated by four positive (Gln3p and Gat1p/Nil1p) and negative (Dal80p/Uga43p and Deh1p/Nil2p/GZF3p) regulators which function in opposition to one another. All four proteins contain GATA-type zinc finger domains, and three of them (Gln3p, Dal80p, and Deh1p) have been shown to bind to GATA sequences situated upstream of genes whose expression is sensitive to nitrogen catabolite repression (NCR). The positive regulators, Gln3p and Gat1p, are able to support transcriptional activation when tethered by LexAp to the promoter of a reporter gene whose upstream activation sequences have been replaced with one or more lexA operator sites. Existing data suggest that these four proteins regulate transcription by competing with one another for binding to the GATA sequences which mediate NCR-sensitive gene expression. We show that the minimal Gln3p domain mediating transcriptional activation consists of 13 amino acids with a predicted propensity to form an ␣-helix. Genetic analysis of this region (Gln3p residues 126 to 138, QQNGEIAQLWDFN) demonstrated that alanine may be substituted for the aromatic and acidic amino acids without destroying transcriptional activation potential. Similar substitution of alanine for the two hydrophobic amino acids, isoleucine and leucine, however, destroys activation, as does introduction of basic amino acids in place of the acidic residues or introduction of proline into the center of the sequence. A point mutation in the Gln3p activation region destroys its in vivo ability to support NCRsensitive DAL5 expression. We find no convincing evidence that NCR regulates Gln3p function by modulating the functioning of its activation region.Four GATA factors mediate regulation of nitrogen catabolic gene expression in Saccharomyces cerevisiae:

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“…Previous studies showed that oligomers of GQ domains possess a high transactivation potential. The Gal4-GQ fusion protein exhibits a dramatic transactivation potential in HeLa cells (14,55). In this case, GQ dimerization is stabilized by dimerization of Gal4 DNA binding motifs.…”

Section: Discussionmentioning

confidence: 99%

“…Lysates were vortexed, sonicated, and cleared by centrifugation at 10,000 ϫ g for 10 min. The cleared lysates were used for immunoprecipitation with anti-SSAP antiserum that was raised against bacterially expressed recombinant SSAP (bSSAP) (14). Typically, 10 l of antiserum was added to the lysate for each 0.1 packed ml of embryos, and the resulting mixtures were incubated on ice for 60 min.…”

Section: Methodsmentioning

confidence: 99%

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Temporal Activation of the Sea Urchin Late H1 Gene Requires Stage-Specific Phosphorylation of the Embryonic Transcription Factor SSAP

Childs

1999

Molecular and Cellular Biology

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Stage-specific activator protein (SSAP) is a 41-kDa polypeptide that binds to embryonic enhancer elements of the sea urchin late H1 gene. These enhancer elements mediate the transcriptional activation of the late H1 gene in a temporally specific manner at the mid-blastula stage of embryogenesis. Although SSAP can transactivate the late H1 gene only at late stages of the development, it resides in the sea urchin nucleus and maintains DNA binding activity throughout early embryogenesis. In addition, it has been shown that SSAP undergoes a conversion from a 41-kDa monomer to a ϳ80-to 100-kDa dimer when the late H1 gene is activated. We have demonstrated that SSAP is differentially phosphorylated during embryogenesis. Serine 87, a cyclic AMP-dependent protein kinase consensus site located in the N-terminal DNA binding domain, is constitutively phosphorylated. At the mid-blastula stage of embryogenesis, temporally correlated with SSAP dimer formation and late H1 gene activation, a threonine residue in the C-terminal transactivation domain is phosphorylated. This phosphorylation can be catalyzed by a break-ended double-stranded DNA-activated protein kinase activity from the sea urchin nucleus in vitro. Microinjection of synthetic SSAP mRNAs encoding either serine or threonine phosphorylation mutants results in the failure to transactivate reporter genes that contain the enhancer element, suggesting that both serine and threonine phosphorylation of SSAP are required for the activation of the late H1 gene. Furthermore, SSAP can undergo blastula-stage-specific homodimerization through its GQ-rich transactivation domain. The late-specific threonine phosphorylation in this domain is essential for the dimer assembly. These observations indicate that temporally regulated SSAP activation is promoted by threonine phosphorylation on its transactivation domain, which triggers the formation of a transcriptionally active SSAP homodimer.

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The embryonic transcription factor stage specific activator protein contains a potent bipartite activation domain that interacts with several RNA polymerase II basal transcription factors.

Cited by 12 publications

References 35 publications

Incorporation of Drosophila TAF110 into the yeast TFIID complex does not permit the Sp1 glutamine‐rich activation domain to function in vivo

Incorporation of Drosophila TAF110 into the yeast TFIID complex does not permit the Sp1 glutamine‐rich activation domain to function in vivo

The minimal transactivation region of Saccharomyces cerevisiae Gln3p is localized to 13 amino acids

Temporal Activation of the Sea Urchin Late H1 Gene Requires Stage-Specific Phosphorylation of the Embryonic Transcription Factor SSAP

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