| First Author | Uegaki K | Year | 1993 |
| Journal | Protein Eng | Volume | 6 |
| Issue | 2 | Pages | 195-200 |
| PubMed ID | 8475044 | Mgi Jnum | J:15789 |
| Mgi Id | MGI:63900 | Doi | 10.1093/protein/6.2.195 |
| Citation | Uegaki K, et al. (1993) Characterization of the DNA binding domain of the mouse IRF-2 protein. Protein Eng 6(2):195-200 |
| abstractText | The DNA binding domain of the interferon regulatory factor-2 protein (IRF-2) has been produced and characterized. alpha-chymotrypsin digestion of the purified IRF-2 protein bound to a synthetic binding site yields a peptide fragment of 14 K in molecular weight. N-terminal analysis of this peptide fragment showed that its sequence is the same as that of the intact IRF-2. A peptide fragment of approximately 14 K, IRF-2(113), which corresponds to the N-terminal 113 amino acids of the intact IRF-2 protein, has been expressed in a functional form in Escherichia coli. The first methionine was processed during the expression and the purified IRF-2(113) thus contains 112 amino acids. DNase I footprinting and gel retardation assaying showed that IRF-2(113) binds to a synthetic DNA having the consensus binding site and to the upstream regulatory sequence of the IFN-beta gene as intact IRF-2 does. These results showed that this peptide fragment, IRF-2(113), may be a good material for investigation of the DNA binding domain of IRF-2 and of the DNA-protein interaction. |
