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Chimeras of herpes simplex viral vp16 and jun are oncogenic

Academic Article
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Overview

authors

  • Schuur, E. R.
  • Parker, E. J.
  • Vogt, Peter K.

publication date

  • September 1993

journal

  • Cell Growth & Differentiation  Journal

abstract

  • The Jun protein binds DNA and regulates transcription as a component of the AP-1 transcription factor complex. In its oncogenic form, Jun can transform cells in culture and cause tumors in animals. Both trans-activation and transformation require several functional domains of Jun, including an amino-terminal trans-activation domain. In this study, properties of Jun required for trans-activation and transformation were explored by replacing the trans-activation domains of c-Jun and its oncogenic counterpart, v-Jun, with the constitutively active trans-activation domain from the herpes simplex virus VP16 protein. The VP16-v-Jun chimera retained similar oncogenic properties to its parent, v-Jun. The VP16-c-Jun chimera, however, was considerably more oncogenic than c-Jun. Substitutions of a phenylalanine in the VP16 domain of the VP16-c-Jun chimera diminished or abolished transformation. Each of the chimeras bound to the AP-1 consensus recognition sequence from the collagenase promoter or from the human T-cell leukemia virus type I long terminal repeat in vitro. None of the VP16-Jun chimeras efficiently stimulated transcription from the collagenase promoter or an artificial promoter containing the human T-cell leukemia virus type I element in vivo. These results demonstrate that the Jun trans-activation domain can be replaced by a heterologous trans-activation domain with retention of oncogenic activity. However, this oncogenic activity is not reflected in the trans-activating properties of the chimeras.

subject areas

  • Animals
  • Base Sequence
  • Cell Line
  • Chick Embryo
  • DNA-Binding Proteins
  • Herpes Simplex Virus Protein Vmw65
  • Molecular Sequence Data
  • Oncogene Protein p65(gag-jun)
  • Recombinant Fusion Proteins
  • Simplexvirus
  • Transcriptional Activation
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Identity

International Standard Serial Number (ISSN)

  • 1044-9523

PubMed ID

  • 8241024
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Additional Document Info

start page

  • 761

end page

  • 768

volume

  • 4

issue

  • 9

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