| First Author | Childs KS | Year | 2003 |
| Journal | Nucleic Acids Res | Volume | 31 |
| Issue | 12 | Pages | 3016-26 |
| PubMed ID | 12799427 | Mgi Jnum | J:83986 |
| Mgi Id | MGI:2664476 | Doi | 10.1093/nar/gkg431 |
| Citation | Childs KS, et al. (2003) Identification of novel co-repressor molecules for Interferon Regulatory Factor-2. Nucleic Acids Res 31(12):3016-26 |
| abstractText | 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. |
