TFE3: a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif.

Beckmann, Holger; Su, Lijuan; Kadesch, Tom

doi:10.1101/gad.4.2.167

Cited by 463 publications

(294 citation statements)

References 77 publications

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“…Since the transcriptional activation of p3TP-Lux by Smad4-HL2 was observed even in the absence of TGF-␤ stimulation, oligomerization and DNA-binding of Smad4-HL2 induced transcriptional activation of p3TP-Lux, although the activity of the Smad4-HL2 oligomer was less than that which was induced by T␤R-I(TD). TFE3 is a basic helix-loop-helix transcription factor which binds to the E-box sequence (Beckmann et al 1990). Although a direct interaction between Smads and TFE3 has not been demonstrated, TFE3 acts in concert with Smads in the transcriptional activation of the PAI-1 promoter, through the binding of both molecules to adjacent sites in the PAI-1 promoter (Hua et al 1998).…”

Section: Discussionmentioning

confidence: 99%

Region between α‐helices 3 and 4 of the Mad homology 2 domain of Smad4: functional roles in oligomer formation and transcriptional activation

et al. 1999

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Background: Smad4 has a unique region of 35 amino acids between ␣-helices 3 and 4 (termed H3/4 loop) of the Mad homology (MH) 2 domain. In order to elucidate the functional importance of the H3/4 loop, we prepared chimeric constructs of Smad4 containing the region corresponding to the ␣-helix 3, H3/4 loop and ␣-helix 4 of different Smads, including a chimera containing that of Smad2 (Smad4-HL2).

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Section: Discussionmentioning

confidence: 99%

Region between α‐helices 3 and 4 of the Mad homology 2 domain of Smad4: functional roles in oligomer formation and transcriptional activation

et al. 1999

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“…Full-length TFE3 (37,38), a truncated TFE3 containing the DNA binding domain (39) and full-length USF (40) were expressed in bacteria as GST fusion proteins. DNase I footprint analysis showed that each protein bound to the E3 element generating a protected region that extended toward the A site (data not shown).…”

Section: Ets and Bhlh Proteins Form A Multiprotein Complex On Thementioning

confidence: 99%

A Three-protein-DNA Complex on a B Cell-specific Domain of the Immunoglobulin μ Heavy Chain Gene Enhancer

Rao

Dang

Tian³

et al. 1997

Journal of Biological Chemistry

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The lymphoid-specific immunoglobulin heavy chain gene intron enhancer ( E) contains multiple binding sites for trans-acting nuclear factors. We have used a combination of in vitro and in vivo assays to reconstruct protein-DNA interactions on a minimal B cell-specific enhancer that contains three motifs, A, B, and E3. Using ETS-domain proteins that transactivate the minimal enhancer in non-lymphoid cells, we show that (i) PU.1 binds coordinately to both A and B sites in vitro and (ii) in the presence of Ets-1, this factor binds to the A site and PU.1 to the B site. Two factors, TFE3 and USF, bind to the E3 element. When the ETS proteins are present together with E3 binding proteins, a threeprotein-DNA complex is generated. Furthermore, we provide evidence for protein-protein interactions between Ets-1 and PU.1 proteins that bind to A and B sites, and between Ets-1 and TFE3 bound to the A and E3 sites. We propose that this domain of the enhancer is assembled into a nucleoprotein complex that contains two tissue-restricted ETS domain proteins that recognize DNA from the same side of the helix and one ubiquitously expressed bHLH-leucine zipper protein that binds between them, recognizing its site from a different side of the helix. The immunoglobulinheavy chain (IgH) gene intron enhancer is a tissue-specific regulatory element that is necessary for expression of the IgH gene (1, 2). Since the proposal of Alt and colleagues of the correlation between transcription and immunoglobulin gene rearrangements (3-5), the enhancer has been considered a likely candidate to be the sequence that regulates rearrangements at this locus. Recently, this hypothesis has been directly verified in mice containing disrupted enhancer alleles (6, 7). Thus, the enhancer is activated at very early stages of B cell differentiation, prior to the onset of D H to J H rearrangements. In addition, experiments in transgenic mice have shown that this enhancer is sufficient to direct expression of heterologous genes in B and T lymphoid cells (8 -11).The enhancer contains binding sites for multiple DNA binding proteins, and tissue-specific activity has been proposed to be the consequence of both positive and negative regulatory proteins. Positive regulation is effected by lymphoid-specific transcription activators, such as those that bind to the A, B (12-15), and octamer elements (16 -18). Negative regulation is effected by proteins found in non-lymphoid cells that may suppress enhancer activity (19 -22), such as those that bind to the E5 site within the enhancer (23, 24). In addition, there are several sites within the enhancer referred to as E motifs. These elements, E1-E5, fit the consensus CANNTG and bind proteins belonging to the basic helix-loop-helix family of transcription factors (25) that are expressed in both lymphoid and nonlymphoid cells. We have previously shown that mutation of either A or B elements abrogates B cell-specific activity of a 170 nucleotide enhancer ( 170) that contains both these elements as well as E1, E3, and E5. Mutati...

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“…Another protein-binding domain, the sequence CACCC, is frequently found in close proximity to the GATA sequence (29) and is located only 7 bp downstream (nt -81 to -85) from the mZP3 GATA sequence. Although the nature and role of the protein that binds to this sequence remain to be determined, it has been suggested that the protein may interact with GATA-binding protein (29 (1,3,6,11). USF has been shown to play a role in transcription of many genes (4,5,12) and apparently acts in concert with the TATA box-binding protein, TFIID (48).…”

Section: Discussionmentioning

confidence: 99%

“…For PR1 the sequence was 5'-CTGA GCCCAGTTGATAATGGGCTCCACCCGAGAG-3' (representing nt -100 to -76 of the mZP3 5'-flanking region and 9 additional 5'-flanking bases). A typical binding reaction mixture (23 gil) contained 0.5 to 1 ng of probe (5,000 cpm), 1 gig of poly(dI-dC) poly(dI-dC), and 2 to 5 gil of crude nuclear extract (2.5 to 6 gig of protein, depending on the extract used) in 25 mM Tris-HCl (pH 7.9)-S50 mM KCl-6.25 mM MgCl2-0.5 mM DTT-10% glycerol. Samples were preincubated for 10 min on ice in the presence of nonspecific DNA competitor, radiolabeled probe was added, and the incubation continued an additional 30 min on ice.…”

Section: Methodsmentioning

confidence: 99%

A mouse oocyte-specific protein that binds to a region of mZP3 promoter responsible for oocyte-specific mZP3 gene expression.

Schickler¹,

Lira²,

Kinloch³

et al. 1992

Mol. Cell. Biol.

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The gene encoding mZP3, the mouse sperm receptor, is expressed exclusively in growing oocytes during oogenesis. To investigate the molecular basis of oocyte-specific mZP3 gene expression, we generated several lines of mice harboring a transgene that contains 470 bp of mZP3 gene 5'-flanking sequence (nucleotides -470 to +10) fused to the firefly luciferase gene coding region. Three of four expressing transgenic lines exhibited luciferase activity only in growing oocytes, suggesting that the 470-bp fragment is sufficient to direct Iocyte-specific expression of the luciferase gene. Results of DNase I footprinting and gel mobility shift assays suggested the presence of an ovary-specific protein that binds to a small region (nucleotides-99 to -86) within the 470-bp fragment of the mZP3 promoter, with 5'-G(G/A)T(G/A)A-3' representing the minimal sequence required for binding. Southwestern (DNA-protein) gel blots revealed the presence of an oocyte-specific, approximately 60,000-Mr protein, called OSP-1, that binds to the minimal sequence. Changes in levels of OSP-1 during oogenesis and early cleavage are consistent with the pattern of mZP3 gene expression during these developmental stages in mice. Therefore, OSP-1 may be a mammalian oocyte-specific transcription factor involved in regulating oocyte-specific mZP3 gene expression.

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TFE3: a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif.

Cited by 463 publications

References 77 publications

Region between α‐helices 3 and 4 of the Mad homology 2 domain of Smad4: functional roles in oligomer formation and transcriptional activation

Region between α‐helices 3 and 4 of the Mad homology 2 domain of Smad4: functional roles in oligomer formation and transcriptional activation

A Three-protein-DNA Complex on a B Cell-specific Domain of the Immunoglobulin μ Heavy Chain Gene Enhancer

A mouse oocyte-specific protein that binds to a region of mZP3 promoter responsible for oocyte-specific mZP3 gene expression.

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