Removing the Vertebrate-Specific TBP N Terminus Disrupts Placental β2m-Dependent Interactions with the Maternal Immune System

Hobbs, Nicole K.; Bondareva, Alla; Barnett, Sheila; Capecchi, Mario R.; Schmidt, Edward E.

doi:10.1016/s0092-8674(02)00806-1

Cited by 37 publications

(66 citation statements)

References 49 publications

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“…The mutant protein contains the entire TBP CORE region of the protein and Western blots confirm that this FLAG-tagged TBP accumulates to wild-type levels in all tissues (34,35). Heterozygous animals are healthy and fertile (34). Survival of animals homozygous for this mutation to E9.5 (100%), birth (9%), and adulthood (ϳ1%) indicates that the FLAG-tagged protein is a functional replacement for most TBP activities (34).…”

Section: Methodsmentioning

confidence: 85%

“…The tbp ⌬N/ϩ mice are heterozygous for a targeted mutation that exchanged the endogenous tbp gene for a version that replaced 111 amino acids within the vertebrate-specific N terminus of TBP with two copies of the FLAG epitope tag (34,35). The mutant protein contains the entire TBP CORE region of the protein and Western blots confirm that this FLAG-tagged TBP accumulates to wild-type levels in all tissues (34,35).…”

Section: Methodsmentioning

confidence: 95%

“…Heterozygous animals are healthy and fertile (34). Survival of animals homozygous for this mutation to E9.5 (100%), birth (9%), and adulthood (ϳ1%) indicates that the FLAG-tagged protein is a functional replacement for most TBP activities (34). Nuclear extracts were prepared to procedures described previously (36,37).…”

Section: Methodsmentioning

confidence: 99%

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Interaction of Protein Inhibitor of Activated STAT (PIAS) Proteins with the TATA-binding Protein, TBP

Prigge

Schmidt

2006

Journal of Biological Chemistry

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Transcription activators often recruit promoter-targeted assembly of a pre-initiation complex; many repressors antagonize recruitment. These activities can involve direct interactions with proteins in the pre-initiation complex. We used an optimized yeast two-hybrid system to screen mouse pregnancy-associated libraries for proteins that interact with TATA-binding protein (TBP). Screens revealed an interaction between TBP and a single member of the zinc finger family of transcription factors, ZFP523. Two members of the protein inhibitor of activated STAT (PIAS) family, PIAS1 and PIAS3, also interacted with TBP in screens. Endogenous PIAS1 and TBP co-immunoprecipitated from nuclear extracts, suggesting the interaction occurred in vivo. In vitro-translated PIAS1 and TBP coimmunopreciptated, which indicated that other nuclear proteins were not required for the interaction. Deletion analysis mapped the PIAS-interacting domain of TBP to the conserved TBP CORE and the TBP-interacting domain on PIAS1 to a 39-amino acid C-terminal region. Mammals issue seven known PIAS proteins from four pias genes, pias1, pias3, piasx, and piasy, each with different cell typespecific expression patterns; the TBP-interacting domain reported here is the only part of the PIAS C-terminal region shared by all seven PIAS proteins. Direct analyses indicated that PIASx and PIASy also interacted with TBP. Our results suggest that all PIAS proteins might mediate situation-specific regulatory signaling at the TBP interface and that previously unknown levels of complexity could exist in the gene regulatory interplay between TBP, PIAS proteins, ZFP523, and other transcription factors. TATA-binding protein (TBP)2 functions in transcription initiation by all three nuclear eukaryotic RNA polymerases (1, 2). TBP-containing complexes include SL1, TFIID, and TFIIIB, which function with RNA polymerase I (RNAPI), RNAPII, and RNAPIII, respectively. RNAPII requires TFIID for promoter-targeted assembly of the pre-initiation complex (3). TBP is also an essential component of the human SNAPc complex, which functions in transcription initiation at small nuclear RNA genes by both RNAPII and RNAPIII (4), and the yeast SAGA complex (5).Recruitment of TBP to the core promoter is regulated by both positive and negative factors (3). Some activators of transcription bind TBP or the TBP-associated factor components of the TFIID complex and direct TFIID to the promoter (6, 7). TBP function can also be up-or down-regulated through interactions with BTAF1/MOT1 and the NC2␣/␤ subunits of the NC2 complex (8, 9). Recently, ZNF76, the human ortholog of mouse zinc finger protein 523 (ZFP523) and of frog Staf (10), was shown to function via direct interaction with TBP (11). The interaction of ZNF76 with TBP is blocked by PIAS1-dependent sumoylation of ZNF76 (11).PIAS proteins are found in all eukaryotes. The human and mouse family of PIAS proteins consists of PIAS1, PIAS3, PIASx, and PIASy proteins (12). The piasx gene encodes two splice variants, PIASx␣/ ARIP3 (androgen receptor...

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Section: Methodsmentioning

confidence: 85%

Section: Methodsmentioning

confidence: 95%

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Interaction of Protein Inhibitor of Activated STAT (PIAS) Proteins with the TATA-binding Protein, TBP

Prigge

Schmidt

2006

Journal of Biological Chemistry

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“…This technique was used successfully to circumvent extraembryonic lethality to produce adult homozygous mutant mice as well as to study the extraembryonic defects themselves (Guillemot et al, 1994). In other studies, this technique was used to bypass extraembryonic defects to study additional embryonic defects (Luo et al, 1997;Rossant et al, 1998;Sibilia et al, 1998;Yamamoto et al, 1998;Li et al, 2000;Gallicano et al, 2001;Hobbs et al, 2002). Diploid embryos aggregated with tetraploid embryos will display the greatest degree of developmental potential, in this case, the diploid cells will be expected to contribute to both embryonic and extraembryonic lineages.…”

Section: Types Of 4n:2n Chimerasmentioning

confidence: 99%

Tetraploid development in the mouse

Eakin

Behringer

2003

Developmental Dynamics

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Spontaneous duplication of the mammalian genome occurs in approximately 1% of fertilizations. Although one or more whole genome duplications are believed to have influenced vertebrate evolution, polyploidy of contemporary mammals is generally incompatible with normal development and function of all but a few tissues. The production of tetraploid (4n) embryos has become a common experimental manipulation in the mouse. Although development of tetraploid mice has generally not been observed beyond midgestation, tetraploid:diploid (4n:2n) chimeras are widely used as a method for rescuing extraembryonic defects. The tolerance of tissues to polyploidy appears to be dependent on genetic background. Indeed, the recent discovery of a naturally tetraploid rodent species suggests that, in rare genetic backgrounds, mammalian genome duplications may be compatible with the development of viable and fertile adults. Thus, the range of developmental potentials of tetraploid embryos remains in large part unexplored. Here, we review the biological consequences and experimental utility of tetraploid mammals, in particular the mouse. Developmental Dynamics 228:751-766, 2003.

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“…Une mutation astucieuse a été introduite dans le domaine aminoterminal du TBP murin [32]. Ce nouvel allèle code pour une protéine TBP tronquée (TBP∆N), constituée principalement de la région carboxyterminale (Figure 2A) …”

Section: Inactivation Du Domaine Aminoterminal De Tbpunclassified

TBP, un facteur de transcription universel ?

2004

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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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Removing the Vertebrate-Specific TBP N Terminus Disrupts Placental β2m-Dependent Interactions with the Maternal Immune System

Cited by 37 publications

References 49 publications

Interaction of Protein Inhibitor of Activated STAT (PIAS) Proteins with the TATA-binding Protein, TBP

Interaction of Protein Inhibitor of Activated STAT (PIAS) Proteins with the TATA-binding Protein, TBP

Tetraploid development in the mouse

TBP, un facteur de transcription universel ?

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