The histone fold is a key structural motif of transcription factor TFIID

Gangloff, Yann-Gaël; Romier, Christophe; Thuault, Sylvie; Werten, Sebastiaan; Davidson, Irwin

doi:10.1016/s0968-0004(00)01741-2

Cited by 132 publications

(145 citation statements)

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“…24,2004 SCAFFOLD FUNCTION OF Taf1p IN TFIID ASSEMBLY 4937 TFIID complex has emerged. New TFIID-specific Tafps have been identified (33,34,60,65,75), novel Tafp-Tafp interactions have been described (22,23,63,66,81), and low-resolution three-dimensional structures of the TFIID complex have been determined (2,11,39,40,48). In this study, we have performed a comprehensive analysis of all the TFIID components associated with Taf1p using co-IP assays and our family of Taf1p deletion mutants that encompass the entire TAF1 ORF.…”

Section: Discussionmentioning

confidence: 99%

“…It is possible that critical conformational changes in TFIID, required for proper functioning (17,20,22,28,30,32,50,53,71), are affected by the mutations in Taf1p-region 4 in the Ts47 mutant. Alternatively, despite the fact that these mutations did not result in total dissociation of the Tafps, they might have sufficiently weakened Tafp-Tafp associations such that the resulting complex displays functional defects.…”

Section: Discussionmentioning

confidence: 99%

“…These TFIID subunits share significant sequence conservation with their metazoan orthologs (1,22,26). In vitro, PolII needs six general transcription factors, TFIIA, -B, -D, -E, -F, and -H, to form functional preinitiation complexes (PICs) (12, 51, 54); TFIID plays several critical roles in this process.…”

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confidence: 99%

“…It was originally hypothesized by Roeder and coworkers (29,53) that a subset of TFIID subunits, those containing the helix-loop-helix-loop-helix or histone fold domain (HFD), could assemble to form a complex resembling the histone nucleosome octamer (1,29,53,60). This core structure was suggested to depend upon the HFD, a structural motif shared by the core histones (22) and many other proteins (70). Nine of 14 yeast Tafps appear to contain HFDs, and subsets of these can form dimers with specific partner HFD Tafps (3,6,9,23,24,29,45,47,80).…”

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confidence: 99%

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Molecular and Genetic Characterization of a Taf1p Domain Essential for Yeast TFIID Assembly

Singh

Bland

Weil

2004

Molecular and Cellular Biology

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Yeast Taf1p is an integral component of the multiprotein transcription factor TFIID. By using coimmunoprecipitation assays, coupled with a comprehensive set of deletion mutants encompassing the entire open reading frame of TAF1, we have discovered an essential role of a small portion of yeast Taf1p. This domain of Taf1p, termed region 4, consisting of amino acids 200 to 303, contributes critically to the assembly and stability of the 15-subunit TFIID holocomplex. Region 4 of Taf1p is mutationally sensitive, can assemble several Tafps into a partial TFIID complex, and interacts directly with Taf4p and Taf6p. Mutations in Taf1p-region 4 induce temperature-conditional growth of yeast cells. At the nonpermissive temperature these mutations have drastic effects on both TFIID integrity and mRNA synthesis. These data are consistent with the hypothesis that Taf1p subserves a critical scaffold function within the TFIID complex. The significance of these data with regard to TFIID structure and function is discussed.TFIID, one of several multiprotein general transcription factors required for RNA polymerase II (PolII)-catalyzed mRNA gene transcription, is comprised of the TATA-binding protein (TBP) and 14 distinct TBP-associated factors (TAFs or Tafps) that range in M r from 17,000 to 150,000 in Saccharomyces cerevisiae (62,63,65,75). These TFIID subunits share significant sequence conservation with their metazoan orthologs (1,22,26). In vitro, PolII needs six general transcription factors, TFIIA, -B, -D, -E, -F, and -H, to form functional preinitiation complexes (PICs) (12, 51, 54); TFIID plays several critical roles in this process. First, TFIID functions during promoter recognition by binding directly to the promoter (67,76,77). On promoters containing a TATA box, Tafps help stabilize TBP binding to the TATA element via interaction with TATA-proximal initiator DNA sequences (69). Tafp-DNA interactions may be particularly important for TFIID binding to promoters that lack a canonical TATA element and contain TATA-proximal initiator and distal promoter element sequences (13,15,42,69,76). Second, Tafps can function as coactivators during transcriptional activation by making direct contacts with specific activators leading to an increase in PolII PIC formation (1, 16). Finally, Taf1p contains several distinct enzymatic activities, those of histone acetyltransferase (HAT) (46), protein kinase (19), and ubiquitin ligase (55). These enzymatic activities presumably modify proteins that stimulate PIC formation and/or function, leading to PolII transcription initiation.In most contexts, the Tafp subunits of TFIID are essential for survival, as Tafp inactivation or depletion results in cessation of specific mRNA synthesis and loss of cell viability (3,4,33,34,56,59,64,65,78). Because of these critical roles, the composition, organization, assembly, structure, and function of the TFIID complex have been topics of great interest. TBP appears to be incorporated into the TFIID complex primarily through its interaction with the biparti...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Molecular and Genetic Characterization of a Taf1p Domain Essential for Yeast TFIID Assembly

Singh

Bland

Weil

2004

Molecular and Cellular Biology

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“…La protéine TBP (TATA binding protein) est un des facteurs clés dans ce processus. En effet, TBP paraît essentiel pour la transcription par les trois ARN polymérases, pol I, pol II et pol III [1][2][3][4][5]. TBP reconnaît l'élément TATA en amont du site d'initiation d'un grand nombre de promoteurs (Figure 1).…”

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TBP, un facteur de transcription universel ?

2004

Self Cite

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L'initiation de la transcription par les ARN polymérases fait intervenir une machinerie complexe, mais conservée au cours de l'évolution. La protéine TBP (TATA binding protein) est un des facteurs clés dans ce processus. En effet, TBP paraît essentiel pour la transcription par les trois ARN polymérases, pol I, pol II et pol III [1][2][3][4][5]. TBP reconnaît l'élément TATA en amont du site d'initiation d'un grand nombre de promoteurs (Figure 1). C'est une protéine bipartite, avec une région aminoterminale variable et un domaine carboxyterminal très conservé. Le domaine aminoterminal présente une importante variabilité de séquence et de taille en fonction des espèces (Figure 2A). Le domaine carboxyterminal est conservé à près de 80% entre la levure et l'homme. Il adopte une structure en «selle de cheval» ( Figure 2D) avec une face concave hydrophobe interagissant avec l'ADN et une face convexe qui interagit avec TFIIA, TFIIB et autres facteurs [6][7][8][9][10]. Sa forte conservation et sa présence dans les complexes d'initiation des trois ARN polymérases ont fait de TBP le «facteur de transcription universel». Des découvertes récentes ont changé notre perspective sur ce caractère universel de TBP. Des protéines apparentées à TBPLa remise en cause du caractère universel de TBP est venue de la découverte de protéines apparentées à TBP. En effet, trois protéines TRF1 (TBP-related factor 1), TLF (TBP-like factor)/TRF2 et TRF3 ont été identifiées et caractérisées [11][12][13][14][15][16][17]. La similarité entre ces protéines est limitée au domaine carboxyterminal conservé (Figure 2A-C TRF1TRF1 n'existe que chez la drosophile où il est exprimé pendant l'embryogenèse puis, de façon spécifique, dans le système nerveux central et les cellules germinales chez l'adulte [16,18]. TRF1 agit comme un facteur de transcription spécifique pour l'expression d'un sous-ensemble de gènes dont Tudor [18]. TRF1 dirige la transcription de Tudor à partir d'un deuxième site d'initiation en amont de celui dirigé par TFIID ( Figure 3A). De plus, TRF1 interagit avec BRF (TFIIB-related factor), un facteur de transcription pol III, et semble se substituer à TBP pour la transcription pol III dans cet organisme [19]. > Le facteur de transcription TBP (TATA-binding protein) est une sous-unité de plusieurs complexes macromoléculaires nécessaires à la transcription par les trois ARN polymérases nucléaires. Cette observation avait conduit à faire de TBP un facteur «universel» de la transcription. La dé-couverte de trois protéines apparentées à TBP, et d'un complexe macromoléculaire dépourvu de TBP, mais capable d'initier la transcription par l'ARN polymérase II in vitro, a conduit à remettre en cause le caractère universel de TBP. Plusieurs études in vivo ont montré que TBP a plutôt un rôle specifique dans l'activation de certains gènes impliqués dans la prolifération cellulaire. De plus, le domaine aminoterminal de TBP joue un rôle dans l'établissement de la tolérance foetomaternelle. <

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