The cellular transcription factor USF cooperates with varicella-zoster virus immediate-early protein 62 to symmetrically activate a bidirectional viral promoter.

Meier, Jeffery L.; Luo, Xu; Sawadogo, Michèle; Straus, Stephen E.

doi:10.1128/mcb.14.10.6896

Cited by 100 publications

(118 citation statements)

References 76 publications

(58 reference statements)

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“…The slight inhibitory e ect of overexpressed dominant mutant DUSF2 on rRNA synthesis may be due to sequestering of endogenous 44 or 43 kDa which causes low level of endogenous 44/43 heterodimer available in the rDNA transcription initiation complex. Such sequestering e ect of USF has also been suggested for the regulation of a bi-directional viral promoter (Meier et al, 1994) and L-type pyruvate kinase gene promoter (Lefrancois Martinez et al, 1995). Co-expression of USF1 and DUSF2 does not alter pol I transcription (data not shown).…”

Section: Discussionmentioning

confidence: 85%

“…pSGU44 or USF2 was constructed by inserting the end-®lled EcoRI ± NsiI fragment of USF44 cDNA (mouse) into BamHI site of pSG5 eucaryotic expression vector (see Lin et al, 1994 and Figure 1D). pSGU44DB or DUSF2 was made by deleting the basic DNA-binding domain (aa 229 to aa 249) of mouse USF2 inserted in pSG5 vector (see Meier et al, 1994 and Figure 1E). pSV-b-Galactosidase (pSV-b-gal) was obtained from Promega.…”

Section: Plasmid Constructsmentioning

confidence: 99%

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The dual role of helix – loop – helix-zipper protein USF in ribosomal RNA gene transcription in vivo

1997

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We have previously demonstrated that the core promoter of rat ribosomal RNA gene (rDNA) contains an E-box-like sequence to which the core promoter binding factor CPBF binds and that the 44 kDa subunit of this protein is immunologically related to USF1, the helix ± loop ± helix-zipper DNA binding protein. Further, we showed that RNA polymerase I (pol I) transcription in vitro is competed by oligonucleotides containing USF-binding site, which suggested a key role for USF in rDNA transcription. To prove the potential role of USF in pol I transcription in vivo, USF1 and USF2 homodimers and USF1/USF2 heterodimer were overexpressed in CHO cells by transfection of the respective cDNAs. Co-transfection of a plasmid containing rDNA followed by primer extension analysis showed that overexpression of USF1 and USF2 as homodimers resulted in inhibition of rDNA transcription by as much as 85 ± 90% whereas overexpression of USF1/USF2 in the heterodimeric form activated transcription approximately 3.5-fold. Transfection of mutant USF2 cDNA that is devoid of the basic DNA-binding domain produced only minimal inhibition of rDNA transcription. These data show that USF can modulate transcription of rRNA gene in vivo by functioning as a repressor (homodimer) or activator (heterodimer) of pol I transcription in vivo and suggest that inhibition of rDNA transcription may be responsible for the antiproliferative action of USF homodimers.

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Section: Discussionmentioning

confidence: 85%

Section: Plasmid Constructsmentioning

confidence: 99%

The dual role of helix – loop – helix-zipper protein USF in ribosomal RNA gene transcription in vivo

1997

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“…Derivation of the pSG5-derived psvUSF1, psvUSF2 and pUSF2DN (pU2DN) expression vectors was previously reported (Meier et al, 1994;Luo and Sawadogo, 1996a,b). Vector alone controls for these expression vectors were provided by transfecting the pSG424 vector containing the same SV40 promoter (Sadowski et al, 1988) instead of the parental pSG5 vector, which, for unknown reasons, strongly inhibited the transcription of cotransfected reporters in several of the cell lines.…”

Section: Plasmidsmentioning

confidence: 99%

Loss of USF transcriptional activity in breast cancer cell lines

1999

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USF is a family of transcription factors that are structurally related to the Myc oncoproteins and also share with Myc a common DNA-binding speci®city. USF overexpression can prevent c-Myc-dependent cellular transformation and also inhibit the proliferation of certain transformed cells. These antiproliferative activities suggest that USF inactivation could be implicated in carcinogenesis. To explore this possibility, we compared the activities of the ubiquitous USF1 and USF2 proteins in several cell lines derived from either normal breast epithelium or breast tumors. The DNAbinding activities of USF1 and USF2 were present at similar levels in all cell lines. In the non-tumorigenic MCF-10A cells, USF in general, and USF2 in particular, exhibited strong transcriptional activities. In contrast, USF1 and USF2 were completely inactive in three out of six transformed breast cell lines investigated, while the other three transformed cell lines exhibited loss of USF2 activity. Analyses in cells cultured from healthy tissue con®rmed the transcriptional activity of USF in normal human mammary epithelial cells. These results demonstrate that a partial or complete loss of USF function is a common event in breast cancer cell lines, perhaps because, like Myc overexpression, it favors rapid proliferation.

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“…A 0.97 kb fragment bearing the ribosomal protein L-30 processed gene (Meyuhas et al, 1987), linking the 5' and 3' regions of the p3A fragment, was used as a control for loading an equivalent amount of total RNA. A 2.2 kb fragment of mouse b-actin (Avni et al, 1994) and a 1.9 kb fragment of USF1 (Meier et al, 1994) were also used as probes for this study. The DNA fragments were labeled with 32 P-dCTP (Amersham) using the random primed labeling technique (Feinberg and Vogelstein, 1983) up to a speci®c activity of 3610 8 c.p.m./mg.…”

Section: Dna Probesmentioning

confidence: 99%

Growth-dependent and PKC-mediated translational regulation of the upstream stimulating factor-2 (USF2) mRNA in hematopoietic cells

Zhang¹,

Nechushtan²,

Jacob‐Hirsch³

et al. 1998

Oncogene

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Upstream stimulating factor (USF2) is a basic helix ± loop ± helix leucine zipper transcription factor, which is found in most tissues. A critical role for USF2 in cellular proliferation has been proposed based on its importance in the regulation of various cyclins and P53 and its capability to antagonize c-myc. In this paper we report that IL-3, which is a major growth factor for mast cells, induces USF2 protein synthesis in murine mast cells . Surprisingly, it does not signi®cantly a ect the level of USF2 mRNA in these cells at any of the time points tested. Using polysomal fractionation and RNA analysis we then demonstrated that this translational regulation is mostly the result of increased USF2 translational e ciency. Moreover, protein kinase C (PKC) inhibitors prevented both the induction of USF2 protein synthesis and the increase in USF2 translational e ciency in IL-3-activated mast cells. Two other hematopoietic cell lines were used to determine whether the translational regulation of USF2 is of a more general nature: mouse lymphosarcoma cells whose proliferation is inhibited by dexamethasone; and mouse erythroleukemia cells that di erentiate upon exposure to hexamethylen bisacetamide. In both cell types, USF2 translation was repressed in the non-dividing cells. This strongly implies that USF2 is translationally repressed in quiescent hematopoietic cells. Considering the proposed role of USF in proliferation it seems that translational regulation of USF2 might have an important role in cellular growth.

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The cellular transcription factor USF cooperates with varicella-zoster virus immediate-early protein 62 to symmetrically activate a bidirectional viral promoter.

Cited by 100 publications

References 76 publications

The dual role of helix – loop – helix-zipper protein USF in ribosomal RNA gene transcription in vivo

The dual role of helix – loop – helix-zipper protein USF in ribosomal RNA gene transcription in vivo

Loss of USF transcriptional activity in breast cancer cell lines

Growth-dependent and PKC-mediated translational regulation of the upstream stimulating factor-2 (USF2) mRNA in hematopoietic cells

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