Nucleic Acids Research, 2003, Vol. 31, No. 12 3016-3026
© 2003 Oxford University Press
Identification of novel co-repressor molecules for Interferon Regulatory Factor-2
Department of Biochemistry and Immunology, St George’s Hospital Medical School, University of London, London SW17 0RE, UK
*To whom correspondence should be addressed. Tel: +44 0208 725 5942; Fax: +44 0208 725 2992; Email: s.goodbourn{at}sghms.ac.uk
We have identified two novel proteins that interact specifically with the C-terminal repression domain of Interferon Regulatory Factor-2 (IRF-2). These proteins, which we term IRF-2 binding proteins 1 and 2 (IRF-2BP1 and IRF-2BP2, the latter having two splicing isoforms, A and B), are nuclear proteins, and have the properties of IRF-2-dependent transcriptional co-repressors that can inhibit both enhancer-activated and basal transcription in a manner that is not dependent upon histone deacetylation. IRF-2BP1 and IRF-2BP2A/B contain an N-terminal zinc finger and a C-terminal RING finger domain of the C3HC4 subclass, but show no homology to other known transcriptional regulators; they therefore define a new family of co- repressor proteins. An alternatively spliced form of IRF-2 that lacks two amino acids (valines 177 and 178) in the central portion of the protein (IRF-2[S]) cannot bind to these co-repressors and cannot mediate repression despite having the same C- terminal repression domain as IRF-2, suggesting that the relative conformation of the DNA binding domain and the C-terminal region of IRF-2 is crucial for transcriptional repression.
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