| First Author | Miura K | Year | 1992 |
| Journal | Biochem Biophys Res Commun | Volume | 187 |
| Issue | 1 | Pages | 375-80 |
| PubMed ID | 1520323 | Mgi Jnum | J:2162 |
| Mgi Id | MGI:50686 | Doi | 10.1016/s0006-291x(05)81503-7 |
| Citation | Miura K, et al. (1992) Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure. Biochem Biophys Res Commun 187(1):375-80 |
| abstractText | We have previously reported that KML1-7 cells cloned from a lupus-prone MRL/l mouse produced a soluble factor that preferentially expanded anti-DNA antibody production across the H-2 barrier. We purified this factor, a 55 kD protein that we termed nucleobindin (Nuc), and obtained its cDNA clone. Although the gene for Nuc encodes a signal peptide and, in fact, Nuc was identified as a secreted protein, Nuc had a DNA-binding property. The putative polypeptide predicted from the cDNA sequence featured a signal peptide, a leucine zipper structure and a basic amino acid-rich region. The DNA-binding property of Nuc was destroyed by deletion of either the leucine zipper structure or the basic amino acid-rich region. The amino acid sequences of Nuc are highly conserved between mouse and human. We discuss the possible role of Nuc in autoimmunity. |
