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Nucleic Acids Research, 2000, Vol. 28, No. 23 4790-4799
© 2000 Oxford University Press

DNA binding and transcription activation by chicken interferon regulatory factor-3 (chIRF-3)

Caroline E. Grant1, Donna L. May1,2 and Roger G. Deeley1,2,3,*

1Cancer Research Laboratories, 2Department of Biochemistry and 3Department of Pathology, Queen’s University, Kingston, Ontario K7L 3N6, Canada

Interferon regulatory factors (IRFs) are a family of transcription factors involved in the cellular response to interferons and viral infection. Previously we isolated an IRF from a chicken embryonic liver cDNA library. Using a PCR-based binding site selection assay, we have characterised the binding specificity of chIRF-3. The optimal binding site (OBS) fits within the consensus interferon-stimulated response element (ISRE) but the specificity of chIRF-3 binding allows less variation in nucleotides outside the core IRF-binding sequence. A comparison of IRF-1 and chIRF-3 binding to ISREs in electrophoretic mobility shift assays confirmed that the binding specificity of chIRF-3 was clearly distinguishable from IRF-1. The selection assay also showed that chIRF-3 is capable of binding an inverted repeat of two half OBSs separated by 10–13 nt. ChIRF-3 appears to bind both the OBS and inverted repeat sites as a dimer with the protein–protein interaction requiring a domain between amino acids 117 and 311. In transfection experiments expression of chIRF-3 strongly activated a promoter containing the OBS. The activation domain was mapped to between amino acids 138 and 221 and a domain inhibitory to activation was also mapped to the C-terminal portion of chIRF-3.

* To whom correspondence should be addressed at: Cancer Research Laboratories, Room A315, Botterell Hall, Queen’s University, Kingston, Ontario K7L 3N6, Canada. Tel: +1 613 533 2778; Fax: +1 613 533 6830; Email: deeleyr{at}post.queensu.ca


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