Abstract:
:Interferons (IFNs) are a family of multifunctional proteins involved in immune activation, regulation of cell growth and antiviral response. They exert their functions by induction of several IFN-stimulated genes, including IFN regulatory factors (IRFs), a family of transcriptional regulators. One of these factors, IRF-2, was initially cloned as an antagonistic counterpart to IRF-1 with oncogenic potential. Here we describe a second isoform of IRF-2, termed IRF-2s, cloned from human and murine cells. This isoform lacks two amino acids located C-terminal of the DNA-binding domain, which is conserved in all IRF family members, leading to a change in the predicted secondary structure. Both isoforms have similar binding affinities to known target sequences in electrophoretic mobility shift assays. Using reporter gene constructs with the type IV promoter region of the MHC class II transactivator (CIITA), which is the essential factor for IFN-gamma-induced MHC class II expression, we show that the short isoform IRF-2s exhibits a weaker activation ability compared to IRF-2. Thus, our data present the first evidence of two IRF-2 isoforms with different regulatory ability.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Koenig Merediz SA,Schmidt M,Hoppe GJ,Alfken J,Meraro D,Levi BZ,Neubauer A,Wittig Bdoi
10.1093/nar/28.21.4219keywords:
subject
Has Abstractpub_date
2000-11-01 00:00:00pages
4219-24issue
21eissn
0305-1048issn
1362-4962journal_volume
28pub_type
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