Activation of the herpes simplex virus immediate-early gene promoters by neuronally expressed POU family transcription factors

Lillycrop, Karen A.; Liu, Y Z; Theil, Thomas; Möröy, Tarik; Latchman, David S.

doi:10.1042/bj3070581

Cited by 15 publications

(17 citation statements)

References 35 publications

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“…The best match to the octamer motif (ATGCAAAT), which binds many POU factors in this region, is the sequence AT-GAAGCT, which shows only a five out of eight match. This therefore confirms and extends previous findings that Brn-3a and Brn-3b can regulate promoter activity by binding to sequences either closely (Lillycrop et al, 1995;Morris et al, 1994) or more distantly (Gerrero et al, 1993;Li et al, 1994;Turner et al, 1994) related to the octamer motif.…”

Section: Discussionsupporting

confidence: 80%

The Different Activities of the Two Activation Domains of the Brn-3a Transcription Factor Are Dependent on the Context of the Binding Site

Budhram-Mahadeo

Morris

Lakin

et al. 1996

Journal of Biological Chemistry

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The POU (Pit-Oct-Unc) family transcription factor Brn-3a contains two distinct activation domains, one at the N terminus of the molecule and one at the C terminus coincident with the DNA binding domain. These different activation domains have been shown previously to differ in their ability to activate an artificial test promoter containing a Brn-3a binding site and the naturally occurring ␣-internexin gene promoter. Here we identify the target site for Brn-3a in the ␣-internexin gene promoter and show that it can confer responsiveness to Brn-3a on a heterologous promoter. One of the single-stranded DNA sequences derived from either this novel Brn-3a binding site or from the previously characterized site in the test promoter are shown to bind Brn-3a preferentially compared with the complementary single strand or the corresponding double-stranded sequence. The pattern of responsiveness of these two sequences when cloned upstream of the same test promoter and co-transfected with constructs encoding various portions of Brn-3a indicates that the activity of the two Brn-3a activation domains is dependent upon differences in the context of the target sequence in each promoter rather than on differences in the target sequence itself.The POU (Pit-Oct-Unc) family of transcription factors play a critical role in the regulation of gene expression in neuronal cells acting by binding to sequences related to the consensus octamer motif ATGCAAAT in the promoters of their target genes (for review, see Verrijzer and van der Vliet (1993) and Wegner et al. (1993)). The Brn-3 family of mammalian POU factors are of particular interest as the mammalian factors most closely related to the nematode POU protein Unc-86 whose inactivation results in the failure to develop specific neuronal cell types particularly sensory neurons (Desai et al., 1988;Finney et al., 1988). Three mammalian Brn-3 factors encoded by distinct genes exist (Theil et al., 1993 and are known as Brn-3a (also known as Brn-3.0: Gerrero et al., 1993;Lillycrop et al., 1992), Brn-3b (also known as Brn-3.2: Lillycrop et al., 1992;Turner et al., 1994), and Brn-3c (also known as Brn-3

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Section: Discussionsupporting

confidence: 80%

The Different Activities of the Two Activation Domains of the Brn-3a Transcription Factor Are Dependent on the Context of the Binding Site

Budhram-Mahadeo

Morris

Lakin

et al. 1996

Journal of Biological Chemistry

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“…2B). This fragment contains, on the negative strand, the sequence TAATGTGAT related to the TAAT-GARAT non-octamer binding site known to be bound by class I, II, III, and IV POU proteins (Aurora and Herr 1992;Certel et al 1996;Cleary and Herr 1995;Hagmann et al 1995;Lillycrop et al 1995). The C fragment also contains an ATGC motif corresponding to the consensus binding site for most POU-s domains.…”

Section: Resultsmentioning

confidence: 99%

Heterospecific transgenesis in Drosophila suggests that engrailed.a is regulated by POU proteins in the crustacean Sacculina carcini

et al. 2002

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Almost all knowledge of the regulation of segmentation genes in arthropods comes from Drosophila. In order to study the regulation of the segment-polarity gene engrailed in a non-insect arthropod we focussed on putative regulatory regions of the engrailed.a (en.a) gene in the barnacle crustacean Sacculina carcini. In this animal, en.ais expressed in segmental stripes like the engrailed genes of other arthropods. As transgenesis in Sacculina is not possible at present, we have used Drosophila as a test tube. The Sacculina en.aintron is able to induce a specific expression of lacZin the Drosophila wing imaginal disc.This pattern is not an engrailed-like pattern, but does suggest that some Drosophila transcription factors interact with the Sacculina en.a intron. We show that two DrosophilaPOU proteins, Nubbin and VVL, and Engrailed itself bind to the Sacculina en.a intron in vitro and that they regulate this expression in vivo. The conservation of POU protein binding sites in metazoans suggests that Sacculina POU proteins could recognize the same sequences. Hence, we looked at the expression of nubbin and vvlhomologues in Sacculinalarvae. Indeed, their expression patterns are consistent with a putative regulatory function on en.a in segments and appendages. Remarkably, the vvl homologue is expressed in Sacculina in a striking striped pattern that is very different from the vvl pattern in Drosophila embryos, and is complementary to the Sacculina en.a pattern. These experiments suggest that the Sacculina engrailed.a gene is regulated by POU proteins.

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“…Oct-1 in association with VP-16 stimulates immediate early gene expression in the herpes simplex virus (61,62), while Oct-2 may inhibit expression of the same genes (63). Other neuronally expressed POU domain genes, including Brn-2 and Brn-3, have been implicated in herpes simplex virus gene expression (64,65). In addition, in vitro studies have demonstrated that several POU domains can regulate replication of adenoviruses (66).…”

Section: Fig 5 Localization Of Skn-1a Binding Sites In the Hpv-1a Lcrmentioning

confidence: 99%

Characterization of Skn-1a/i POU Domain Factors and Linkage to Papillomavirus Gene Expression

Andersen¹,

Pittelkow²,

Rosenfeld³

1997

Journal of Biological Chemistry

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Tissue-restricted POU domain transcription factors, which bind octamer or octamer-like gene sequences, play roles in cellular differentiation and the development of several organs. We have previously identified a POU domain gene, Skn-1a/i, expressed primarily in epidermis, that encodes at least two products through alternative splicing. One of these, Skn-1a, acts as a transcriptional activator, and the other, Skn-1i, contains an inhibitory domain in the NH 2 terminus, which prevents DNA-binding in vitro and transcriptional activation in vivo. We now demonstrate that when Skn-1i is expressed in eukaryotic cells it can bind to an octamer site, suggesting that in vivo cellular factors modulate the activity of the inhibitory domain to permit DNA-binding. Yet the inhibitory domain does not allow transactivation by Skn-1i or by a heterologous transactivator containing this domain in cis. Furthermore, we demonstrate that Skn-1a, Tst-1, and Oct-1 are the major octamer-binding proteins in epidermis. Since Skn-1a is primarily expressed in suprabasal cells of the epidermis, we have tested its possible role in the regulation of epidermal papillomaviruses. In transient transfection assays, Skn-1a and Tst-1 can activate the long control region of the epidermis-specific human papillomavirus 1A (HPV-1A). Consistent with these in vivo transcription data, in vitro DNA binding studies identify three octamer-like sites, which are capable of binding Skn-1a, in the HPV-1A long control region. Mutations of all three octamer-like sites prevent transactivation by Skn-1a in transient transfection assays. Taken together, these results provide evidence that Skn-1a and Tst-1 may provide a molecular link between HPV gene expression and epidermal differentiation.During midgestation in mammals, the embryo is enclosed by a cellular bilayer composed of a basal layer of somatic ectoderm, which is covered by distinct epithelial cells referred to as periderm. While periderm is later shed, somatic ectoderm has several distinct fates in the mature organism. These fates include mammary epithelium, teeth, epidermis, and epidermal appendages such as hair, nails, and sweat glands (1). Epidermis, which forms relatively late in embryogenesis, is made of a single layer of proliferating basal keratinocytes and several layers of postmitotic suprabasal cells. The basal keratinocytes express a pair of keratins, K5 and K14, but, concomitant with departure from the basal layer, they exit the cell cycle, suppress expression of K5 and K14, and induce expression of another keratin pair, K1 and K10. As keratinocytes move outward to the surface of the skin, proteins required for formation of a cornified cell envelope are induced. These cells subsequently undergo programmed cell death to form the cornified layer of the epidermis. This differentiation process, first initiated during embryogenesis, continues throughout life with cell proliferation in the basal layer balanced by cell death and eventual shedding of the stratum corneum (2).Human papillomaviruses (HPVs) 1 ar...

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Activation of the herpes simplex virus immediate-early gene promoters by neuronally expressed POU family transcription factors

Cited by 15 publications

References 35 publications

The Different Activities of the Two Activation Domains of the Brn-3a Transcription Factor Are Dependent on the Context of the Binding Site

The Different Activities of the Two Activation Domains of the Brn-3a Transcription Factor Are Dependent on the Context of the Binding Site

Heterospecific transgenesis in Drosophila suggests that engrailed.a is regulated by POU proteins in the crustacean Sacculina carcini

Characterization of Skn-1a/i POU Domain Factors and Linkage to Papillomavirus Gene Expression

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