Specific interaction between a transcription factor and the upstream element of the adenovirus-2 major late promoter.

Miyamoto, Neil G.; Moncollin, Vincent; Egly, Jean‐Marc; Chambon, Pierre

doi:10.1002/j.1460-2075.1985.tb04118.x

Cited by 196 publications

(140 citation statements)

References 47 publications

(82 reference statements)

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“…Our data point strongly to a USF heterodimer being the predominant factor that binds to this particular E-box. USF was originally identi®ed as a human cellular factor which bound to an E-box motif in the adenovirus major late promoter and which stimulated transcription in in vitro assays (Carthew et al, 1987;Miyamoto et al, 1985;Sawadogo and Roeder, 1985). Bendall and Molloy (1994) performed a detailed analysis of E-box¯anking sequences in order to identify the determinants for Myc/Max versus USF speci®city.…”

Section: Discussionmentioning

confidence: 99%

Isolation and initial characterization of the BRCA2 promoter

et al. 1999

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The hereditary breast cancer susceptibility gene, BRCA2, is considered to be a tumor suppressor gene that may be involved in the cellular response to DNA damage. The transcript for this gene is cell cycle regulated with mRNA levels reaching a peak just before the onset of DNA synthesis. In order to de®ne the mechanisms by which BRCA2 is transcriptionally regulated, we have begun to study upstream regulatory sequences. In this report, we de®ne a minimal promoter region that has strong activity in human breast epithelial cells. Deletions of this sequence narrowed the strong basal activity to a region extending from 766 to +129 with respect to the BRCA2 transcriptional start site. This sequence demonstrated cell cycle regulated activity with kinetics similar to the endogenous transcript. Examination of the sequence revealed several consensus binding sites for transcription factors including an E-box, E2F and Ets recognition motifs. Electrohoretic mobility shift assays revealed speci®c protein binding to two sequences upstream of the start site; the palindromic Ebox and an Ets/E2F site. Site-directed mutagenesis of either of these sites reduced both the basal activity in log phase cells and the cell cycle regulated activity of the promoter. Mutational inactivation of both sites within the same construct eectively eliminated promoter activity. Antibodies to candidate transcription factors used in super shift experiments revealed speci®c interactions between the BRCA2 promoter and the basic region/helix ± loop ± helix containing USF-1 and 2 proteins and Elf-1, an Ets domain protein. Binding of these factors depended upon the presence of intact recognition sequences. The USF factors were shown to bind predominantly as a heterodimeric complex of USF-1 and 2 while Elf-1 bound the promoter when it was not occupied by USF. Co-transfection studies with USF proteins and the varicella zoster IE62 protein provide evidence for the involvement of endogenous and exogenous USF in the activation of the BRCA2 promoter. We propose that interactions between USF-1, USF-2 and Elf-1 play an important role in the transcriptional regulation of the BRCA2 gene.

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Section: Discussionmentioning

confidence: 99%

Isolation and initial characterization of the BRCA2 promoter

et al. 1999

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“…The finding that USF bound the HLH-OB2 enhancer was somewhat unexpected since USF has a fairly well established consensus binding site of CACGTG (25)(26)(27), which differs in the central dinucleotide from the CT/CGRP HLH-OB2 HLH motif of CAGCTG. This latter sequence is preferably recognized by the E12 and myoD class of HLH proteins, not the USF proteins (46).…”

Section: Activity Of the Ct/cgrp Enhancer In The Context Of Flanking mentioning

confidence: 99%

“…The E12/E47 and ITF-2 proteins have been shown to functionally interact with homeodomain proteins to help direct cell-specific gene expression (22)(23)(24). The USF proteins were initially identified as upstream stimulatory factors that control the adenovirus major late promoter (25)(26)(27). Since then, USF binding sites have been found in a number of cellular genes (28 -33).…”

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confidence: 99%

Binding of Upstream Stimulatory Factor and a Cell-specific Activator to the Calcitonin/Calcitonin Gene-related Peptide Enhancer

Lanigan

Russo

1997

Journal of Biological Chemistry

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The calcitonin/calcitonin gene-related peptide (CT/ CGRP) gene is selectively transcribed in thyroid C cells and neurons. We have previously shown that the rat CT/CGRP cell-specific enhancer is synergistically regulated by a helix-loop-helix (HLH) protein and the OB2 octamer-binding protein. In this report, we show that the HLH-OB2 enhancer is required for full promoter activity, even in the context of other HLH elements.Since this enhancer appears to be a major controlling element, we have characterized the HLH and OB2 DNA binding proteins. We have identified the major HLH complex as a heterodimer of the ubiquitous upstream stimulatory factor (USF)-1 and USF-2 proteins. USF bound the enhancer with a reasonably high affinity (K D 1.6 nM), comparable to other genes. Characterization of a series of mutations revealed that a portion of the HLH motif is also recognized by OB2 and confirmed that HLH activity requires OB2. We have shown that OB2 is a single DNA binding protein based on UV cross-linking studies. The 68-kDa protein-DNA complex was detected only in C cell lines, including a human C cell line that has robust HLH-OB2 enhancer activity. These results suggest that the calcitonin/CGRP gene is controlled by the combinatorial activity of a ubiquitous USF HLH heterodimer and an associated cell-specific activator.

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“…Altogether, these studies have identified three promoter elements; the upstream activating element (UAE) centered at position -63 to -52, the TATA box located at position -31 to -25, and the initiator at position -6 to + 4. Sawadogo and Roeder (1985) and others (Carthew et al 1985;Miyamoto et al 1985) have described a cellular factor, upstream stimulatory factor (USF, or MLTFI or UEF) that both stimulates transcription of the AdML promoter up to 10-fold in vitro and binds to an upstream element that is essential for this stimulation. Glycerol gradient sedimentation studies indicate a size of 45-60 kD for USF (Chodosh et al 1986;Moncollin et al 1986).…”

mentioning

confidence: 99%

The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer.

Gregor¹,

Sawadogo²,

Roeder³

1990

Genes Dev.

570

442

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We isolated full-length cDNAs encoding the 43-kD form of human upstream stimulatory factor (USF), a cellular factor required for efficient transcription of the adenovirus major late (AdML) promoter in vitro. Sequence analysis showed USF to be a member of the c-myc-related family of DNA-binding proteins. Using proteins translated in vitro, we identified a DNA-binding domain near the carboxyl terminus, which includes both a helix-loop-helix motif and a leucine repeat. We show that USF interacts with its target DNA as a dimer. The leucine repeat is required for efficient DNA binding of the intact protein and for interactions between fulllength and truncated USF proteins. Interestingly, it is not required for DNA binding of the isolated helix-loophelix domain. The structure of different cDNA clones indicates that USF RNA is differentially spliced, and alternative exon usage may regulate the levels of functional USF protein.

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Specific interaction between a transcription factor and the upstream element of the adenovirus-2 major late promoter.

Cited by 196 publications

References 47 publications

Isolation and initial characterization of the BRCA2 promoter

Isolation and initial characterization of the BRCA2 promoter

Binding of Upstream Stimulatory Factor and a Cell-specific Activator to the Calcitonin/Calcitonin Gene-related Peptide Enhancer

The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer.

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