Human TAFII105 Is a Cell Type–Specific TFIID Subunit Related to hTAFII130

Dikstein, Rivka; Zhou, Shi-Sheng; Tjian, Robert

doi:10.1016/s0092-8674(00)81330-6

Cited by 165 publications

(174 citation statements)

References 37 publications

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“…In addition to the 8-12 ubiquitously expressed TAFs, recent reports have identified tissue-specific TAF homologs in both Drosophila and mammals. Although only one tissue-specific TAF has been characterized in mammals [TAF4b (20)], five tissue-specific TAF homologs have been described in Drosophila (21,22). These tissue-specific TAFs are expressed in the developing spermatocytes within the testis and are termed no hitter (nht), cannonball (can), meiosis I arrest (mia), spermatocyte arrest (sa), and ryan express (rye), which are cell-type-specific homologs of TAF4, TAF5, TAF6, TAF8, and TAF12, respectively.…”

Section: Discussionmentioning

confidence: 99%

TAF4 nucleates a core subcomplex of TFIID and mediates activated transcription from a TATA-less promoter

Wright

Marr

Tjian

2006

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

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137

146

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Activator-dependent recruitment of TFIID initiates formation of the transcriptional preinitiation complex. TFIID binds core promoter DNA elements and directs the assembly of other general transcription factors, leading to binding of RNA polymerase II and activation of RNA synthesis. How TATA box-binding protein (TBP) and the TBP-associated factors (TAFs) are assembled into a functional TFIID complex with promoter recognition and coactivator activities in vivo remains unknown. Here, we use RNAi to knock down specific TFIID subunits in Drosophila tissue culture cells to determine which subunits are most critical for maintaining stability of TFIID in vivo. Contrary to expectations, we find that TAF4 rather than TBP or TAF1 plays the most critical role in maintaining stability of the complex. Our analysis also indicates that TAF5, TAF6, TAF9, and TAF12 play key roles in stability of the complex, whereas TBP, TAF1, TAF2, and TAF11 contribute very little to complex stability. Based on our results, we propose that holo-TFIID comprises a stable core subcomplex containing TAF4, TAF5, TAF6, TAF9, and TAF12 decorated with peripheral subunits TAF1, TAF2, TAF11, and TBP. Our initial functional studies indicate a specific and significant role for TAF1 and TAF4 in mediating transcription from a TATA-less, downstream core promoter element (DPE)-containing promoter, whereas a TATA-containing, DPE-less promoter was far less dependent on these subunits. In contrast to both TAF1 and TAF4, RNAi knockdown of TAF5 had little effect on transcription from either class of promoter. These studies significantly alter previous models for the assembly, structure, and function of TFIID.RNA interference ͉ TATA box-binding protein ͉ S2 cells R egulated initiation of transcription to produce mRNA in eukaryotes requires the stepwise assembly of an elaborate multiprotein preinitiation complex consisting of the general transcription factors, various coactivators, and RNA polymerase II (for review, see ref. 1). The core promoter-recognition complex, TFIID, consists of the TATA box-binding protein (TBP) and 8-12 TBP-associated factors (TAFs). In addition to binding core promoter elements and initiating formation of the preinitiation complex, this TBP⅐TAF multisubunit transcription factor also serves as a coactivator by transmitting signals from sequence-specific activators to other components of the basal machinery (for review, see ref.2).Critical to dissecting the diverse functions of TFIID in both promoter recognition and coactivation is an understanding of how the complex is assembled and maintained in cells. Initial in vitro assembly reactions suggested that TBP and the largest TAF subunit (TAF1) may form a scaffold on which the other TAFs bind to form holo-TFIID (3). Subsequent studies have proposed that TAF5 may dimerize and also help coordinate complex assembly (4). Recent low-resolution electron microscopy͞single-particle reconstruction models of TFIID have revealed a trilobed architecture containing a large central cavity that has been conse...

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Section: Discussionmentioning

confidence: 99%

TAF4 nucleates a core subcomplex of TFIID and mediates activated transcription from a TATA-less promoter

Wright

Marr

Tjian

2006

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

Self Cite

137

146

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“…Their synthesis would represent another mechanism for modifying TFIID structure and function, besides post-translation modi®cations of TBP and TAF II s (Boyer and Berk, 1993;Segil et al, 1996) and the selective addition of cell-and promoter-speci®c subunits (Jacq et al, 1994;Bertolotti et al, 1996;Dikstein et al, 1996). Less likely, they could be mRNA molecules with a di erent primary structure but sharing a common motif, as hypothesized for the various transcripts detected by the 5' segment of TBP cDNA (Purrello et al, 1994a, and unpublished results).…”

Section: Northern Analysis Of Taf II Transcriptsmentioning

confidence: 99%

Genomics and transcription analysis of human TFIID

et al. 1998

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TFIID, a multisubunit protein comprised of TBP (TATA box-binding protein) and TAF II s (TBP-associated factors), has a central role in transcription initiation at class II promoters. TAF II s role as mediators of regulatory transcription factors, such as pRb and p53, and their involvement in signal transduction pathways suggest that some may participate in the control of cell proliferation and di erentiation: therefore, they could be considered potential protooncogenes or antioncogenes. With the aim of starting to analyse these potential roles, we have determined the genomic position of nine human TAF II genes (TAF II 250, TAF II 135, TAF II 100, TAF II 80, TAF II 55, TAF II 43, TAF II 31, TAF II 28, TAF II 20/15) and of two previously unknown sequences related to TAF II 250 and TAF II 31, respectively. Except for those encoding TAF II 250 and TAF II 31, these genes are present in a single copy and, with the exclusion of those for TAF II 43 and TAF II 28 (both at 6p21), are localized in di erent segments of the genome. Indeed, six of them map to a chromosomal region commonly altered in speci®c neoplasias, which de®nes them as candidates for involvement in oncogenesis. Our experiments also demonstrate that TAF II transcripts are synthesized ubiquitously, mostly at low levels similar to those of TBP. Interestingly, the amount of the major mRNA species detected by TAF II 20/15 cDNA is higher, which suggests that the polypeptide it encodes may also perform functions independently of TFIID. TAF II isoforms, indicated by additional bands on Northern blots, may play a role in modulation of TFIID function. These data will be useful for analysing variations of TAF II mRNA phenotype during cell proliferation, di erentiation and development, both normal and pathological.

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“…Domain I, contained within ETO-2 residues 146 ± 242, has previously been shown to have limited homology to a Drosophilia transcription accessory factor, TAF110 (Feinstein et al, 1995). This TAF-related domain is common to several TAFs isolated from vertebrates, including hTAFII 135, hTAFII 130 and the related hTAFII 105 (Tanese et al, 1996;Dickstein et al, 1996). Domain II (ETO-2 residues 371 ± 402) is a leucine-rich region that apparently mediates homo-and heterodimerization between the ETO family of proteins ( Figure 5).…”

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confidence: 99%

ETO-2, a new member of the ETO-family of nuclear proteins

et al. 1999

Oncogene

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The t(8;21) is associated with 12 ± 15% of acute myelogenous leukemias of the M2 subtype. The translocation results in the fusion of two genes, AML1 (CBFA2) on chromosome 21 and ETO (MTG8) on chromosome 8. AML1 encodes a DNA binding factor; the ETO protein product is less well characterized, but is thought to be a transcription factor. Here we describe the isolation and characterization of ETO-2, a murine cDNA that encodes a new member of the ETO family of proteins. ETO-2 is 75% identical to murine ETO and shares very high sequence identities over four regions of the protein with ETO (domain I ± III and zinc-®nger). Northern analysis identi®es ETO-2 transcripts in many of the murine tissues analysed and in the developing mouse embryo. ETO-2 is also expressed in myeloid and erythroid cell lines. We con®rmed the nuclear localization of ETO-2 and demonstrated that domain III and the zinc-®nger region are not required for nuclear localization. We further showed that a region within ETO, containing domain II, mediates dimerization among family members. This region is conserved in the oncoprotein AML-1/ETO. The recent identi®cation of another ETO-like protein, myeloid translocation generelated protein 1, together with the data presented here, demonstrates that at least three ETO proteins exist with the potential to form dimers in the cell nucleus.Keywords: ETO family; MTG8; (8;21) translocation; nuclear; dimerization Of the many chromosomal translocations associated with acute myelogenous leukemia (AML), the t(8;21) is one of the most common, accounting for approximately 15% of the M2 subtype (Rowley, 1984). This translocation results in the fusion of the AML1 (CBFA2) gene on chromosome 21 and the ETO (MTG8) gene on chromosome 8. The resultant hybrid gene-product, AML-1/ETO, is comprised of the ®rst 177 amino acids of AML-1 and includes all but the ®rst 30 amino acids of the ETO (MTG8b) protein (Erickson et al., 1992;Kozu et al., 1993;Miyoshi et al., 1993). AML-1/ETO, expressed from the AML1 promoter, is thought to be central to leukemogenesis as its reciprocal chimeric mRNA and protein have not been observed.AML1 encodes several alternatively spliced transcription factors; AML-1 (250 aa), AML-1b (453 aa), Correspondence: S Meyers Received 27 May 1998; revised 7 September 1998; accepted 8 September 1998Figure 1 ETO-2 is a new member of the ETO-family of proteins. (a) The amino acid sequence of murine ETO-2 (mETO-2). The regions of highest conservation among family members were de®ned by using the multiple sequence alignment program Pileup and are underlined. The asterisks (*) denote every tenth amino acid. The sequence data reported here has been deposited in the GenBank sequence databases under the accession number AFO38029. A mouse spleen cDNA library constructed in the Lambda Zap II bacteriophage vector was plated and screened according to the manufacturer's directions (Stratagene). The DNA sequence of both strands of the cDNA was determined by primer walking using dideoxy-chain termination and double stranded DNA ...

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Human TAFII105 Is a Cell Type–Specific TFIID Subunit Related to hTAFII130

Cited by 165 publications

References 37 publications

TAF4 nucleates a core subcomplex of TFIID and mediates activated transcription from a TATA-less promoter

TAF4 nucleates a core subcomplex of TFIID and mediates activated transcription from a TATA-less promoter

Genomics and transcription analysis of human TFIID

ETO-2, a new member of the ETO-family of nuclear proteins

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