Interaction between an acidic activator and transcription factor TFIIB is required for transcriptional activation

Roberts, Stefan G. E.; Ha, Ilho; Maldonado, Edio; Reinberg, Danny; Green, Michael R.

doi:10.1038/363741a0

Cited by 226 publications

(210 citation statements)

References 18 publications

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“…Different laboratories have demonstrated in vitro protein-protein interactions between the VP16 activation domain and several general transcription factors, including TATA-binding protein (TBP) (49), TFIIB (34), TFIIH (53), a TBP-associated factor (17), and the RNA polymerase II holoenzyme (19). Mutations which affect binding to the VP16 activation domain and reduce activated but not basal transcription in vitro have been isolated in two factors, TBP and TFIIB (27,46). Importantly, VP16 activation mutants with amino acid substitutions of F442 are defective for in vitro interactions with TBP (21) and with TFIIH (53), suggesting that F442 may play an important role in protein-protein interactions crucial to the activation process.…”

Section: Discussionmentioning

confidence: 99%

Extensive Mutagenesis of a Transcriptional Activation Domain Identifies Single Hydrophobic and Acidic Amino Acids Important for Activation In Vivo

Sainz

Goff

Chandler

1997

Molecular and Cellular Biology

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C1 is a transcriptional activator of genes encoding biosynthetic enzymes of the maize anthocyanin pigment pathway. C1 has an amino terminus homologous to Myb DNA-binding domains and an acidic carboxyl terminus that is a transcriptional activation domain in maize and yeast cells. To identify amino acids critical for transcriptional activation, an extensive random mutagenesis of the C1 carboxyl terminus was done. The C1 activation domain is remarkably tolerant of amino acid substitutions, as changes at 34 residues had little or no effect on transcriptional activity. These changes include introduction of helix-incompatible amino acids throughout the C1 activation domain and alteration of most single acidic amino acids, suggesting that a previously postulated amphipathic ␣-helix is not required for activation. Substitutions at two positions revealed amino acids important for transcriptional activation. Replacement of leucine 253 with a proline or glutamine resulted in approximately 10% of wild-type transcriptional activation. Leucine 253 is in a region of C1 in which several hydrophobic residues align with residues important for transcriptional activation by the herpes simplex virus VP16 protein. However, changes at all other hydrophobic residues in C1 indicate that none are critical for C1 transcriptional activation. The other important amino acid in C1 is aspartate 262, as a change to valine resulted in only 24% of wild-type transcriptional activation. Comparison of our C1 results with those from VP16 reveal substantial differences in which amino acids are required for transcriptional activation in vivo by these two acidic activation domains.

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Section: Discussionmentioning

confidence: 99%

Extensive Mutagenesis of a Transcriptional Activation Domain Identifies Single Hydrophobic and Acidic Amino Acids Important for Activation In Vivo

Sainz

Goff

Chandler

1997

Molecular and Cellular Biology

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“…This conformation of TFIIB could more efficiently recruit the other proximal basal factors for initiation. Such a conformational change in TFIIB has been postulated {Choy and Green 1993; Roberts and Green 1994}, and mutants in TFIIB exist that support basal but not stimulated transcription (Roberts et al 1993}. It is also likely that the activated TFIID-TFIIA-template conformation preferentially interacts with basal factors beyond TFHB in initiation.…”

Section: Genes and Developmentmentioning

confidence: 93%

Activation of the TFIID-TFIIA complex with HMG-2.

Shykind¹,

Kim²,

Sharp³

1995

Genes Dev.

139

102

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The nonhistone chromosomal protein HMG-2 was identified as a factor necessary for activation in a defined transcription reaction in vitro containing RNA polymerase II and purified factors. Activation occurred on all promoters assayed except that of the immunoglobulin IgH gene. TFIIA was required for stimulated levels of transcription. The activation process depended on the presence of TAFs in the TFIID complex and generated a preinitiation complex from which TFIIB dissociated more slowly. However, titration of TFIIB over three orders of magnitude did not obviate the requirement of activator and HMG-2 to achieve stimulated levels of transcription. Analysis of the activated reaction identified the TFIID-TFIIA complex as the first stage of modification during activation. These results suggest that activation can occur solely in the presence of the basal factors, activator protein, and an "architectural" HMG factor, which probably stabilizes an activated conformation of the TFllD-TFIIA-promoter complex.[Key Words: HMG-1/2; transcriptional activation; coactivator] Received March 13, 1995; revised version accepted April 21, 1995.The basal reaction for initiation of transcription by RNA polymerase II (Pol II) can be reconstituted with distinct protein factors that assemble on the promoter in an ordered fashion (for review, see Buratowski 1994). This process is nucleated by recognition of the TATA element by TFIID (or the TATA-binding protein, TBP) and culminates, alter assembly, with conversion of the initiation complex into the elongation complex. The basal factors required for this reaction have been purified to homogeneity, and the genes for many have been cloned. On promoters such as the adenovirus major late [MLP), this set of factors is comprised of TFIID, TFIIB, TFIIE, TFIIF, TFIIH, and Pol II. The factors TFIIA and TFIIJ can stimulate the basal reaction (Samuels et al. 1982;Cortes et al.

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“…According to this idea, these activating regions merely have to perform a ''glue-like'' function, and in principle any of a variety of activatormachinery interactions could suffice for, or be involved in, activation. Consistent with this idea, an array of potential targets in the transcriptional machinery have been found to interact with activating regions in vitro, including TATA box-binding protein (TBP), TFIIB, SRB4, certain TBPassociated factors, TFIIH, and the Ada-Gcn5 and Swi͞Snf complexes, and for some of these interactions there are corresponding genetic experiments that support the idea that they are physiologically relevant (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25).…”

mentioning

confidence: 86%

An artificial transcriptional activating region with unusual properties

Ansari

Ptashne

2000

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

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We describe a series of transcriptional activators generated by adding amino acids (eight in one case, six in another) to fragments of the yeast Saccharomyces cerevisiae activator Gal4 that dimerize and bind DNA. One of the novel activating regions identified by this procedure is unusual, compared with previously characterized yeast activating regions, in the following ways: it works more strongly than does Gal4's natural activating region as assayed in yeast; it is devoid of acidic residues; and several lines of evidence suggest that it sees targets in the yeast transcriptional machinery at least partially distinct from those seen by Gal4's activating region.

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Interaction between an acidic activator and transcription factor TFIIB is required for transcriptional activation

Cited by 226 publications

References 18 publications

Extensive Mutagenesis of a Transcriptional Activation Domain Identifies Single Hydrophobic and Acidic Amino Acids Important for Activation In Vivo

Extensive Mutagenesis of a Transcriptional Activation Domain Identifies Single Hydrophobic and Acidic Amino Acids Important for Activation In Vivo

Activation of the TFIID-TFIIA complex with HMG-2.

An artificial transcriptional activating region with unusual properties

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