A novel PRD I and TG binding activity involved in virus-induced transcription of IFN-A genes (original) (raw)

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Laboratoire de Reègulation de I'Expression des Geènes Eucaryotes, CNRS, UPR, 37, UFR Biomeédicale des Saints-Peères, Universiteé Reneé Descartes

45 rue des Saints-Peères, 75270 Paris Cedex 06, France

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Laboratoire de Reègulation de I'Expression des Geènes Eucaryotes, CNRS, UPR, 37, UFR Biomeédicale des Saints-Peères, Universiteé Reneé Descartes

45 rue des Saints-Peères, 75270 Paris Cedex 06, France

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,

Laboratoire de Reègulation de I'Expression des Geènes Eucaryotes, CNRS, UPR, 37, UFR Biomeédicale des Saints-Peères, Universiteé Reneé Descartes

45 rue des Saints-Peères, 75270 Paris Cedex 06, France

Search for other works by this author on:

,

Laboratoire de Reègulation de I'Expression des Geènes Eucaryotes, CNRS, UPR, 37, UFR Biomeédicale des Saints-Peères, Universiteé Reneé Descartes

45 rue des Saints-Peères, 75270 Paris Cedex 06, France

Search for other works by this author on:

Laboratoire de Reègulation de I'Expression des Geènes Eucaryotes, CNRS, UPR, 37, UFR Biomeédicale des Saints-Peères, Universiteé Reneé Descartes

45 rue des Saints-Peères, 75270 Paris Cedex 06, France

* To whom correspondence should be addressed

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Published:

01 January 1995

Accepted:

03 November 1995

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Pierre Geènin, Jose Bragança, Nicole Darracq, Janine Doly, Ahmet civas, A novel PRD I and TG binding activity involved in virus-induced transcription of IFN-A genes, Nucleic Acids Research, Volume 23, Issue 24, 25 December 1995, Pages 5055–5063, https://doi.org/10.1093/nar/23.24.5055
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Abstract

Comparative analysis of the inducible elements of the mouse interferon A4 and A11 gene promoters (IE-A4 and IE-A11) by transient transfection experiments, DNase I footprinting and electrophoretic mobility shift assays resulted in identification of a virus-induced binding activity suggested to be involved in NDVinduced activation of transcription of these genes. The virus-induced factor, termed VIF, is activated early by contact of virions with cells. It specifically recognizes the PRD Mike domain shared by both inducible elements, as well as the TG-like domain of IE-A4. This factor, distinct from the IRF-1, IRF-2 and the aF1 binding proteins and presenting a different affinity pattern from that of the TG protein, is proposed as a candidate for IFN-type I gene regulation.

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