High impact information on IRF1

• The cloning and functional characterization of a novel interferon regulatory factor (IRF), IRF-10, are described [1].
• The 5'-upstream region of the cloned ChIFN1 gene contains two putative binding sites for IRF-1, but lacks NF-kappaB-binding sites, and it did not respond well to virus in transfected cells [2].
• The chicken fibroblast cell line C32 has been transfected with the chicken homolog (Ch-IRF-1) of the mammalian transcription factor IRF-1 [3].
• The IRF-1 proteins from primary chicken embryo fibroblasts (CEF) and CEC-32 cells differed in their electrophoretic mobility [4].
• The deduced amino acid sequences of IRF-1 cDNA from chicken and quail show high similarity [4].

Biological context of IRF1

• Both type I and II IFNs, as well as dsRNA and IRF-1, trans-activate the promoter in short-term transfection experiments [5].
• A cloned flounder interferon regulatory factor (designated fIRF) cDNA was found to be 1746 bp in length, with an open reading frame of 297 amino acids [6].

Other interactions of IRF1

• In contrast to that of IRF-1, which has some of the same functional characteristics, the expression of IRF-10 is not cytotoxic for fibroblasts or B cells [1].
• Amino acid sequence identities between the DNA-binding domain of the fIRF and that of both chicken IRF-1 and chicken IRF-2 were 72.3% [6].

Analytical, diagnostic and therapeutic context of IRF1

• Molecular cloning of a novel interferon regulatory factor in Japanese flounder, Paralichthys olivaceus [6].
• 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 [7].

References