Identification of USF as the ubiquitous murine factor that binds to and stimulates transcription from the immunoglobulin λ2 chain promoter

Chang, Ling A.; Smith, T. A.; Pognonec, Philippe; Roeder, Robert G.; Murialdo, Helios

doi:10.1093/nar/20.2.287

Cited by 23 publications

(12 citation statements)

References 39 publications

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“…USF has been shown to bind to the consensus E-box sequences and activate the expression of class I alcohol dehydrogenase (42), type I plasminogen activator inhibitor (46), immunoglobulin X2-chain promoter (12), and p53 tumor suppressor (44) genes. In addition, USF has also been shown to bind to and stimulate the transcription of y-fibrinogen (16) (58), which regulate muscle-specific genes and the developmental effects of retinoic acid in vivo, respectively.…”

Section: Discussionmentioning

confidence: 99%

The basic helix-loop-helix protein upstream stimulating factor regulates the cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements.

et al. 1994

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Previous studies have documented that 250 bp of the rat cardiac ventricular myosin light-chain 2 (MLC-2v) promoter is sufficient to confer cardiac muscle-specific expression on a luciferase reporter gene in both transgenic mice and primary cultured neonatal rat myocardial cells. Utilizing ligation-mediated PCR to perform in vivo dimethyl sulfate footprinting, the present study has identified protein-DNA interaction within the position from -176 to -165. This region, identified as MLE1, contains a core sequence, CACGTG, which conforms to the consensus E-box site and is identical to the upstream stimulating factor (USF)-binding site of the adenovirus major late promoter. Transient assays of luciferase reporter genes containing point mutations of the site demonstrate the importance of this cis regulatory element in the transcriptional activation of this cardiac muscle gene in ventricular muscle cells. The protein complex that occupies this site is capable of binding to HF-la and PRE B sites which are known to be required for cardiac muscle-specific expression of rat MLC-2v and a-myosin heavy-chain genes, respectively. This study provides direct evidence that USF, a member of the basic helix-loop-helix leucine zipper family, binds to MLE1, HF-la, and PRE B sites and suggests that it is a component of protein complexes that may coordinately control the expression of MLC-2v and a-myosin heavy-chain genes. The current study also provides evidence that USF can positively and negatively regulate the MLC-2v gene via independent cis regulatory elements.

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Section: Discussionmentioning

confidence: 99%

The basic helix-loop-helix protein upstream stimulating factor regulates the cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements.

et al. 1994

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“…Specifically, we have compared the properties of USF1, which constitutes the predominant E3 DNA binding activity in nuclear extracts (11,37), and TFE3, previously shown to be an activator of IgH enhancer-based reporters (6,35). We demonstrate that, in contrast to the transcriptional activation mediated by TFE3, overexpression of either USF1 or Max leads to transcriptional inhibition.…”

mentioning

confidence: 94%

Selective Utilization of Basic Helix-Loop-Helix–Leucine Zipper Proteins at the Immunoglobulin Heavy-Chain Enhancer

Carter

Ordentlich

Kadesch

1997

Molecular and Cellular Biology

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The E3 E box within the immunoglobulin heavy-chain (IgH) enhancer binds several proteins of the basic helix-loop-helix-leucine zipper (bHLHzip) class, including TFE3, USF1, and Max. Both TFE3 and USF have been described as transcriptional activators, and so we investigated their possible roles in activating the IgH enhancer in vivo. Although TFE3 activated various enhancer-based reporters, both USF1 and Max effectively inhibited transcription. Inhibition by USF correlated with the lack of a strong activation domain and was the result of the protein neutralizing the E3 site. The effects of dominant-negative derivatives of TFE3 and USF1 confirmed that TFE3, or a TFE3-like protein, is the primary cellular bHLHzip protein that activates the IgH enhancer. In addition to providing a physiological role for TFE3, our results call into question the traditional view of USF1 as an obligate transcriptional activator.B-cell-specific transcription of the immunoglobin heavychain (IgH) locus is directed primarily by an enhancer located within the intron separating the J and C regions of the gene. Transfection experiments and in vitro binding studies have defined numerous sites within an approximately 250-bp region critical for enhancer activity. Among the proteins that bind these sites are two cell-restricted proteins (Oct-2 and PU.1) and several additional transcription factors of the basic helixloop-helix (bHLH), bHLH-leucine zipper (bHLHzip), ets, zinc finger, and POU-homeodomain families (for a review, see reference 24). Previous work in this laboratory has identified a 60-bp region containing three E boxes (E5, E2, and E3) that generates B-cell-specific activity in transfected cells (35). Two of the E boxes, E5 and E2, bind members of the bHLH family of transcription factors, including the products of the E2A (E12 and E47 [32-34]), E2-2 (22), and HEB (23) genes. The E2A proteins are major determinants of lymphoid development, as deletion of the E2A gene leads to a complete loss of the B-cell lineage in mice (4, 39). Although the E47 protein is widely expressed, DNA binding by E47 homodimers is restricted to B cells (36). DNA binding by E47 in certain other cell types requires dimerization with distinct cell-restricted bHLH partners such as MyoD (28,33).Transfection of E47 expression plasmids results in the activation of various E-box-containing reporters and, additionally, the chromosomal IgH locus in non-B cells (12). E47 homodimers have been shown to competitively displace a repressor protein from the E5 site (18). In the absence of this E47-mediated derepression, the repressor inhibits activity that would otherwise be generated through widely expressed proteins that bind other enhancer sites, including the neighboring E3 site (35). The E3-binding proteins identified thus far are members of the bHLHzip family and include TFE3 (5), USF1 (20), TFEB (10), Myc:Max heterodimers (8, 27), and Max homodimers (7,8). Although TFE3, USF1, and Myc:Max heterodimers have all been described as activators at E3-like elements, it is uncl...

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“…The recognition sequence of USF is present in promoters of a number of cellular genes (Bresnick and Felsenfeld, 1993;Chang et al, 1992;Cogswell et al, 1995;Outram and Owen, 1994;Read et al, 1993;Reisman and Rotter, 1993;Wang and Sul, 1995). USF is a member of the bHLHZip family and exhibits closely related characteristics to another bHLHZip family member, Myc.…”

Section: Introductionmentioning

confidence: 99%

Cross-family interaction between the bHLHZip USF and bZip Fra1 proteins results in down-regulation of AP1 activity

Pognonec¹,

Boulukos²,

Aperlo³

et al. 1997

Oncogene

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Heterodimerization among the basic-leucine zipper (bZIP) proteins or among the basic-helix ± loop ± helixleucine zipper (bHLHZip) proteins confers a multitude of combinational activities to these transcription factors. To further examine the function of the bHLHZip protein, USF, we screened for cellular proteins which could directly interact with USF using the yeast two-hybrid system. A bZip protein, Fra1, was found to e ciently interact with USF. USF speci®cally interacts with Fra1 but not with other closely related family members, c-Fos, Fra2, FosB, or with c-Jun. Both the bHLHZip and the N-terminal regions of Fra1 are required for e cient interaction with USF. In vivo association between USF and Fra1 has been demonstrated by co-immunoprecipitation. Expression of exogenous USF led to a decrease in AP1-dependent transcription in F9 cells. Co-expression of exogenous Fra1 restored the AP1 activity in a dosedependent manner. These data show that USF and Fra1 physically and functionally interact demonstrating that cross-talk occurs between factors of distantly related transcription families.

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Identification of USF as the ubiquitous murine factor that binds to and stimulates transcription from the immunoglobulin λ2 chain promoter

Cited by 23 publications

References 39 publications

The basic helix-loop-helix protein upstream stimulating factor regulates the cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements.

The basic helix-loop-helix protein upstream stimulating factor regulates the cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements.

Selective Utilization of Basic Helix-Loop-Helix–Leucine Zipper Proteins at the Immunoglobulin Heavy-Chain Enhancer

Cross-family interaction between the bHLHZip USF and bZip Fra1 proteins results in down-regulation of AP1 activity

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