Identification of novel co-repressor molecules for Interferon Regulatory Factor-2.

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.
Mesh Terms:
Alternative Splicing, Amino Acid Sequence, Binding Sites, Carrier Proteins, Cloning, Molecular, DNA, Complementary, DNA-Binding Proteins, Gene Silencing, HeLa Cells, Histone Deacetylase Inhibitors, Humans, Interferon Regulatory Factor-2, Molecular Sequence Data, Nuclear Proteins, Protein Isoforms, Protein Structure, Tertiary, Repressor Proteins, Sequence Alignment, Transcription Factors, Transcription, Genetic
Nucleic Acids Res.
Date: Jun. 15, 2003
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