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Nucleic Acids Res. 1995 Dec 25;23(24):5055-63.

A novel PRD I and TG binding activity involved in virus-induced transcription of IFN-A genes.

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Laboratoire de Régulation de l'Expression des Gènes Eucaryotes, CNRS, UPR 37, UFR Biomédicale des Saints-Pères, Université René Descartes, Paris, France.


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 1 footprinting and electrophoretic mobility shift assays resulted in identification of a virus-induced binding activity suggested to be involved in NDV-induced 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 I-like 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 alpha F1 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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