Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains

Berger, Shelley L.; Piña, Benjamı́n; Silverman, Neal S.; Marcus, Gregory A.; Agapite, Julie; Regier, J L; Triezenberg, Steven J.; Guarente, Leonard

doi:10.1016/0092-8674(92)90100-q

Cited by 425 publications

(451 citation statements)

References 69 publications

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“…Expression of CBF1 in yeast was accomplished by ligating restriction fragments encoding CBF1 (the BclI-BglII and BglII-BglII fragments from pACT-11) into the BglII site of pDB20.1 (kindly provided by S. Triezenberg; ref. 20), bringing CBF1 under control of the yeast ADC1 promoter.…”

Section: Methodsmentioning

confidence: 99%

Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit

Stockinger

Gilmour

Thomashow

1997

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

1,588

1,203

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Recent efforts have defined a cis-acting DNA regulatory element in plants, the C-repeat͞dehydration responsive element (DRE), that stimulates transcription in response to low temperature and water deficit. Here we report the isolation of an Arabidopsis thaliana cDNA that encodes a C-repeat͞DRE binding factor, CBF1 (C-repeat͞DRE Binding Factor 1). Analysis of the deduced CBF1 amino acid sequence indicates that the protein has a molecular mass of 24 kDa, a potential nuclear localization sequence, and a possible acidic activation domain. CBF1 also has an AP2 domain, which is a DNA-binding motif of about 60 aa present in the Arabidopsis proteins APETALA2, AINTEGUMENTA, and TINY; the tobacco ethylene response element binding proteins; and numerous other plant proteins of unknown function. The transcript levels for CBF1, which appears to be a single or low copy number gene, did not change appreciably in plants exposed to low temperature or in detached leaves subjected to water deficit. Binding of CBF1 to the C-repeat͞DRE was demonstrated in gel shift assays using recombinant CBF1 protein expressed in Escherichia coli. Moreover, expression of CBF1 in yeast was found to activate transcription of reporter genes containing the C-repeat͞DRE as an upstream activator sequence but not mutant versions of the DNA element. We conclude that CBF1 can function as a transcriptional activator that binds to the C-repeat͞DRE DNA regulatory element and, thus, is likely to have a role in cold-and dehydrationregulated gene expression in Arabidopsis.

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Section: Methodsmentioning

confidence: 99%

Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit

Stockinger

Gilmour

Thomashow

1997

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

1,588

1,203

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“…Acidic activation domains in general, and VP16 in particular, are of interest in that they are not only very efficient activators of target promoter elements but also unusual in being fully functional in both lower and higher eukaryotes, thus implying that their mechanism of action has been conserved over considerable evolutionary distances (38). On the other hand, recent genetic data for S. cerevisiae have also demonstrated that acidic activation domains can be divided into at least two functionally distinct subclasses (3), thus raising the question of whether VP16 is indeed a representative model for this entire class of activation domains.…”

mentioning

confidence: 99%

“…As a more rigorous test of this hypothesis, we have taken advantage of the finding that acidic activators of the VP16 type are characterized by a high degree of dependence on the expression of ADA2, a putative transcriptional adaptor protein, for biological activity in yeast cells (3). In contrast, some other acidic transcriptional activators, such as the yeast HAP4 protein, are only modestly affected by the lack of ADA2 function.…”

mentioning

confidence: 99%

“…In contrast, the observation that overexpression of activation domains can result in the inhibition (squelching) of activated but not basal transcription has been interpreted to mean that these domains are titrating out a protein that is distinct from these general factors (2,12,29,46). Potential candidate proteins for this coactivator or adaptor role include the TBP-associated factors (TAFs) (15,21) as well as two proteins termed ADA2 and ADA3 that have been shown to be required for acidic activation domain function in the yeast Saccharomyces cerevisiae (3,34 has been the acidic class, and particularly the activation domain of the prototypic VP16 transcriptional activator encoded by herpes simplex virus (35,48,49). Acidic activation domains in general, and VP16 in particular, are of interest in that they are not only very efficient activators of target promoter elements but also unusual in being fully functional in both lower and higher eukaryotes, thus implying that their mechanism of action has been conserved over considerable evolutionary distances (38).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Mutational analysis of the transcription activation domain of RelA: identification of a highly synergistic minimal acidic activation module.

Blair¹,

Bogerd²,

Madore³

et al. 1994

Mol. Cell. Biol.

107

124

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The potent C-terminal activation domain of the RelA(p65) subunit of the cellular transcription factor NF-KB is shown to contain several discrete acidic activation modules. These short, -11-amino-acid modules were able to give rise to only a low level of transcription activation when fused to the GAL4 DNA-binding domain as monomers. However, dimers and higher-order multimers activated the transcription of minimal promoter elements as effectively as the full-length RelA or VP16 activation domain. Therefore, this 11-aminoacid ReIA-derived acidic module appears to contain all of the sequence information required to fully activate a target promoter element as long as it is presented in a form that permits functional synergy. Critical primary sequence requirements for acidic activation module function included a core phenylalanine residue and flanking bulky hydrophobic residues. Overall negative charge was necessary but not sufficient for function. While dimeric forms of the 11-amino-acid acidic activation module bound to either TFIIB or TATA-binding protein efficiently in vitro, a similarly charged peptide lacking the core phenylalanine residue failed to interact.Overall, these data demonstrate that the biological activity of the RelA activation domain is dependent on acidic activator sequences that are closely comparable to those detected in the activation domain of the viral VP16 regulatory protein. We hypothesize that the ability of these acidic activators to specifically interact with multiple components of the transcription initiation complex likely underlies the dramatic functional synergy exhibited by this class of activation domains in vivo.

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“…The GCN5p/ADA2p/ADA3p activator complex was identified using a distinct type of genetic screen carried out by Guarente and colleagues to identify mutations in genes that confer resistance to the toxic chimeric transcriptional activator GAL4-VP16 (Berger et al 1992). Genes identified by this screen might be involved in facilitating gene activation by the VP16 acidic activation domain.…”

Section: Activators and Repressors: Genetic Definition In S Cerevisiaementioning

confidence: 99%

Activators and repressors: making use of chromatin to regulate transcription

1997

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Metazoans and yeast use enzymes that modulate histone acetylation and nucleosomal integrity in order to regulate transcription. Repressor complexes deacetylate histones and stabilize nucleosomes. Activator complexes acetylate histones and disrupt nucleosomes. Variation in chromatin structure makes a major contribution to gene regulation. Here we discuss the enzymatic complexes and molecular machines that make use of chromatin to control transcription.

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Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains

Cited by 425 publications

References 69 publications

Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit

Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit

Mutational analysis of the transcription activation domain of RelA: identification of a highly synergistic minimal acidic activation module.

Activators and repressors: making use of chromatin to regulate transcription

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