The avian erythroblastosis virus erbA oncogene encodes a DNA-binding protein exhibiting distinct nuclear and cytoplasmic subcellular localizations

Boucher, Philip E.; Koning, A. P. Jason de; Privalsky, Martin L.

doi:10.1128/jvi.62.2.534-544.1988

Cited by 47 publications

(19 citation statements)

References 56 publications

(106 reference statements)

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“…DNA binding assays. To test the capability of pp38 protein to bind to DNA, double-stranded DNA-cellulose (Sigma) was used as previously described (2). Briefly, 100 ,ul of total-cell lysate (50 x 106/ml) was mixed with DNA-binding buffer (20 mM Tris-HCl [pH 8.2], 10% glycerol, 0.1 M NaCl, and 0.1 mM dithiothreitol) containing a 10% slurry of DNAcellulose.…”

Section: Methodsmentioning

confidence: 99%

Structural analysis and transcriptional mapping of the Marek's disease virus gene encoding pp38, an antigen associated with transformed cells

Cui

Lee

Liu

et al. 1991

J Virol

100

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The gene encoding a Marek's disease virus (MDV) pp38 phosphoprotein has been identified, sequenced, and localized to the BamHI H fragment to the left of the putative MDV origin of replication. The open reading frame was defined by sequencing of a lacZ-pp38 fusion protein gene from a Agt 1 expression library. The entire open reading frame is 290 amino acids long and codes for a protein with a calculated molecular weight of 31,169, compared with the size of 38 kDa of the phosphorylated form estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Si nuclease protection analysis showed that the pp38 gene is transcribed leftward as an unspliced mRNA. On the basis of transcriptional mapping studies, the pp38 transcript is predicted to be about 1.8 kb in length without a poly(A) sequence. Its promoter-enhancer region overlaps that of the major rightward BamHI H 1.8-kb transcript implicated in tumor induction. This region

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Section: Methodsmentioning

confidence: 99%

Structural analysis and transcriptional mapping of the Marek's disease virus gene encoding pp38, an antigen associated with transformed cells

Cui

Lee

Liu

et al. 1991

J Virol

100

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“…Similarly, a major role for silencing is demonstrated by the chicken oncogene product v-erbA. It does not bind T3 due to mutations in its ligand binding domain (14), it functions as a constitutive silencer protein (6,11,12,15) and it interferes with normal erythropoiesis (16)(17)(18)(19)(20). A natural mutant of v-erbA (Pro 399 to Arg) lacks the oncogenic and the silencing activity (21,22).…”

Section: Introductionmentioning

confidence: 99%

Two silencing sub-domains of v-erbA synergize with each other, but not with RXR

1994

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The thyroid hormone receptor (TR) and the retinoic acid receptor (RAR) induce gene expression in the presence of specific ligand and repress transcription in the absence of hormone. This repression is mediated by an active silencing mechanism rather then by interference with DNA binding activators. V-erbA, a variant form of TR which is unable to bind hormone, represents a constitutive repressor. Here we show, using fusion proteins with the GAL4 DNA binding domain, that the minimal silencing domain of v-erbA extends from amino acids 389 to 632 and that internal deletions within this domain retain at least some repression function. Co-transfection experiments of different deletion mutants indicate that the silencing domain is composed of at least two sub-domains which are non-functional when tested individually. When combined in a heterodimeric complex, they synergize such that silencing activity is regained. In contrast to the retinoic acid receptor the retinoid X receptor does not contain a silencing domain. In addition it is unable to cooperate with the repression function of TR or v-erbA in a heterodimer.

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“…By analyzing the ligand-binding capacities of proteins representing chimeras between the normal receptor and p75 gag v-erbA, it has been shown that several mutations present in the carboxy terminal half of the protein cooperate in abolishing hormone binding (1 1,12). V-erbA is, however, localised to the nucleus and appears to bind DNA in vitro (9,13). Thus it can be postulated that v-erbA acts on gene transcription by a mechanism similar to its cellular counterpart, i.e.…”

Section: Introductionmentioning

confidence: 99%

The lack of transcriptional activation of the v-erbA oncogene is in part due to a mutation present in the DNA binding domain of the protein

Verneuil

Metzger²

1990

Nucleic Acids Research

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Using a transient co-transfection system we have demonstrated that response elements for estrogen (ER), thyroid hormone (TR) and retinoic acid receptors (RAR) are closely related. Thyroid hormone-induced activation of transcription was observed in CV1 cells and not in HeLa cells, suggesting the existence of cell-specific transcription factors necessary for the response. By contrast to its cellular counterpart (c-erbA/cTR alpha) the oncogene protein gag v-erbA is unable to activate gene transcription from different response elements derived from the rat growth hormone (rGH) gene promoter. A chimeric construct consisting of the ER in which the DNA binding domain has been replaced by that of cTR alpha was able to stimulate the reporter gene. In contrast, a construct in which ER DNA binding domain has been replaced by that of gag v-erbA did not activate gene transcription. These results lead us to the conclusion that the mutated DNA binding domain of v-erbA is in part responsible for the lack of transcriptional activation and in repression of gene expression. This is due in large part to the Gly73----Ser mutation which corresponds to the position of one of the three discriminating amino acids that are thought to interact with a specific base of the response element.

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The avian erythroblastosis virus erbA oncogene encodes a DNA-binding protein exhibiting distinct nuclear and cytoplasmic subcellular localizations

Cited by 47 publications

References 56 publications

Structural analysis and transcriptional mapping of the Marek's disease virus gene encoding pp38, an antigen associated with transformed cells

Structural analysis and transcriptional mapping of the Marek's disease virus gene encoding pp38, an antigen associated with transformed cells

Two silencing sub-domains of v-erbA synergize with each other, but not with RXR

The lack of transcriptional activation of the v-erbA oncogene is in part due to a mutation present in the DNA binding domain of the protein

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