PEA1 and PEA3 enhancer elements are primary components of the polyomavirus late transcription initiator element

Yoo, Won Sang; Martin, Mark; Folk, William R.

doi:10.1128/jvi.65.10.5391-5400.1991

Cited by 37 publications

(15 citation statements)

References 81 publications

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“…The stretch of DNA between the Inr sequence and the A ⁄ T-rich region in the DPP-III promoter contains a GC box (Sp1-binding motif) and two Ets-1 ⁄ Elk-1-binding motifs. Both of these transcription factors are known to help in recruitment of the transcription initiation assembly [27][28][29] and therefore this arrangement of nucleotides in the DPP-III promoter is probably responsible for the strong promoter activity of DPP-III in U87MG cells. Deletion analysis of the DPP-III promoter revealed that the region between )781 and )485 bp contains several transcription factor binding motifs such as USF, C ⁄ EBP and Sp1 (Fig.…”

Section: Discussionmentioning

confidence: 99%

Ets‐1/ Elk‐1 is a critical mediator of dipeptidyl‐peptidase III transcription in human glioblastoma cells

2010

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Dipetidyl‐petidase III is a metallopeptidase involved in a number of physiological processes and its expression has been reported to increase with the histological aggressiveness of human ovarian primary carcinomas. Because no information regarding the regulation of its expression was available, experiments were designed to clone, define and characterize the promoter region of the human dipeptidyl‐peptidase III (DPP‐III) gene. In this study, we cloned a 1038 bp 5′‐flanking DNA fragment of the human DPP‐III gene for the first time and demonstrated strong promoter activity in this region. Deletion analysis revealed that as few as 45 nucleotides proximal to the transcription start site retained ∼ 40% of the activity of the full‐length promoter. This promoter lacked the TATA box but contained multiple GC boxes and a single CAAT box. Similarly, two Ets‐1/Elk‐1‐binding motifs are present in the first 25 nucleotides from the transcription start site. Binding of Ets‐1/Elk‐1 proteins to these motifs was visualized by electrophoretic mobility shift and chromatin immunoprecipitation assays. Mutations of these binding sites abolished not only binding of the Ets protein, but also the intrinsic promoter activity. Increased DNA‐binding activity of Ets‐1/Elk‐1 by v‐Ha‐ras also augmented the mRNA level and promoter activity of this gene. Similarly, co‐transfection of DPP‐III promoter–reporter constructs with Ets‐1 expression vector led to a significant increase in promoter activity. From these results, we conclude that Ets‐1/Elk‐1 plays a critical role in transcription of the human DPP‐III gene.

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Section: Discussionmentioning

confidence: 99%

Ets‐1/ Elk‐1 is a critical mediator of dipeptidyl‐peptidase III transcription in human glioblastoma cells

2010

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“…5, 3' deletion from the position +65 to +31 slightly increased the CAT expression, suggesting the presence of a weak repressing sequence in this deleted region. Each of the internal deletions of the putative E2F-binding sequence [28], the tran- scription-initiation site and the putative PEA3-binding sequence [29] decreased the CAT expression, suggesting the important roles of these sequences in promoter function. As shown in Fig.…”

Section: Mapping Of the Target Region In The Pcna Gene Promoter For Rmentioning

confidence: 99%

Differential effect of p53 on the promoters of mouse DNA polymerase β gene and proliferating‐cell‐nuclear‐antigen gene

Yamaguchi

Hayashi

Matsuoka

et al. 1994

European Journal of Biochemistry

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A plasmid carrying the 5' flanking region of the mouse proliferating-cell-nuclear-antigen (PCNA) gene or DNA polymerase p gene was fused with the chloramphenicol acetyltransferase (CAT) gene, then cotransfected into mouse N18TG2 cells with the expression plasmid for the pS3 gene. Expression of the wild-type p53 repressed the CAT expression directed by the PCNA gene promoter, while it had little effect on the DNA polymerase p gene promoter. RNase protection analysis revealed that the repression of the PCNA gene promoter by p53 was at the transcription step. Analysis with various deletion mutants in the PCNA gene promoter revealed that a specific sequence is not required for the repression, suggesting that p53 represses the PCNA gene promoter by interacting with some components of the basic transcription machinery. By analysis with various deletion mutants in the DNA polymerase p gene promoter, we identified the unique 10-bp palindromic sequence (-24 to -1S), in the presence of which p.53 was not able to repress the promoter activity. This sequence conferred resistance to p53 repression onto the PCNA gene promoter, when it was placed 21 -bp upstream from the transcription-initiation site.The product of the tumor-suppressor p53 gene is a nuclear phosphoprotein involved in the control of cell proliferation, and mutations in the p53 gene are associated with diverse types of human cancer [l-31. It is tempting to postulate that pS3 functions as a guardian of the genome [4]. When DNA is damaged by mutagenic agents such as ultraviolet light, the level of p53 elevates to arrest cells at G1 phase, so that the damaged DNA can be repaired during this arresting period [4-61. Mutant type p53, however, is not able to induce G1 arrest of cells, and therefore, permits replication of damaged DNA. Consequently, accumulated lesions in DNA can cause the death or transformation of cells. Although the molecular mechanism of G1 arrest induced by wild-type pS3 is not clear, pS3 probably functions as a transcription factor. Wild-type p53 binds to specific DNA sequences [7-91, and stimulates transcription when these binding sites are close to a minimal promoter [lo-141. Wild-type p53 also negatively regulates a variety of genes that lack a p53-binding sequence, probably by interacting with the general transcription-factorlike TATA-binding protein [ 121. Considering all these observations, it would be interesting to compare the effect of p.53 on DNA-replication-related genes with that on DNA-repairrelated genes.DNA polymerase is one of five cellular DNA polymerases in vertebrates [15-171. The role of this enzyme has Correspondence to A. Matsukage,

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“…NIH 3T3 cells were transfected with DNA by calcium phosphate coprecipitation and glycerol shock as previously described (83) or with Lipofectamine (20 l of Lipofectamine/60-mm-diameter plate) per directions by Gibco-BRL. MOP-3T3 and MOP-3T6 cells were transfected with DNA with Lipofectamine, and COS1 cells were transfected with Lipofectace (Gibco-BRL).…”

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confidence: 99%

Tiny T antigen: an autonomous polyomavirus T antigen amino-terminal domain

Riley

Yoo

Mda

et al. 1997

J Virol

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Three mRNAs from the murine polyomavirus early region encode the three well-characterized tumor antigens. We report the existence of a fourth alternatively spliced mRNA which encodes a fourth tumor antigen, tiny T antigen, which comprises the amino-terminal domain common to all of the T antigens but is extended by six unique amino acid residues. The amount of tiny T antigen in infected cells is small because of its short half-life. Tiny T antigen stimulates the ATPase activity of Hsc70, most likely because of its DnaJ-like motif. The common amino-terminal domain may interface with chaperone complexes to assist the T antigens in carrying out their diverse functions of replication, transcription, and transformation in the appropriate cellular compartments. The small, middle, and large T antigens expressed by the murine polyomavirus (muPy) are formed of a common aminoterminal sequence juxtaposed to unique carboxy-terminal sequences (33, 65). Such parsimony in protein structures reflects the pattern of viral gene expression, for the T antigens are encoded by a single primary transcript containing two splice acceptor and two splice donor sites (76) (Fig. 1), creating the potential of four separate mRNAs. Three of these RNAs encode the small, middle, and large T antigens. The fourth mRNA, heretofore undetected, should encode a protein with the T antigen common amino-terminal domain extended by six residues. Here, we report the detection of this mRNA and the partial characterization of the protein it encodes (tiny T antigen). Genetic and biochemical evidence indicates the muPy T antigen common amino-terminal domain is required for cell transformation and promotes small and middle T antigen association with PP2A, c-Src, and perhaps other proteins (5, 26, 73). These cellular signal transducers strongly influence viral DNA replication, transcription, and translation; consequently, the T antigen common amino-terminal domain must contribute to virtually all aspects of the virus life cycle. Sequence homology between the T antigen amino-terminal domain and DnaJ proteins has been noted (36). DnaJ proteins modulate the ATPase activity of the hsp70 class of chaperones, and we observe that tiny T antigen expressed in Escherichia coli and purified to near homogeneity exhibits such a stimulatory activity in vitro. This activity within the T antigen amino-terminal domain very likely contributes to the functions of the T antigens by promoting their interactions with cellular chaperones. MATERIALS AND METHODS Cells and viruses. NIH 3T3, 3T6, and COS1 cells were obtained from the American Type Culture Collection. Polyomavirus transformed MOP-3T3 and MOP-3T6 cells were obtained from John Hassell (McMaster University, Ontario, Canada). Whole mouse embryo (WME) cells were prepared from outbred mice as described previously (24). All cells were grown in Dulbecco's modified Eagle's medium (low glucose) supplemented with 10% fetal calf serum.

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PEA1 and PEA3 enhancer elements are primary components of the polyomavirus late transcription initiator element

Cited by 37 publications

References 81 publications

Ets‐1/ Elk‐1 is a critical mediator of dipeptidyl‐peptidase III transcription in human glioblastoma cells

Ets‐1/ Elk‐1 is a critical mediator of dipeptidyl‐peptidase III transcription in human glioblastoma cells

Differential effect of p53 on the promoters of mouse DNA polymerase β gene and proliferating‐cell‐nuclear‐antigen gene

Tiny T antigen: an autonomous polyomavirus T antigen amino-terminal domain

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