| First Author | Kiefer SM | Year | 2002 |
| Journal | J Biol Chem | Volume | 277 |
| Issue | 17 | Pages | 14869-76 |
| PubMed ID | 11836251 | Mgi Jnum | J:76167 |
| Mgi Id | MGI:2178733 | Doi | 10.1074/jbc.M200052200 |
| Citation | Kiefer SM, et al. (2002) Murine sall1 represses transcription by recruiting a histone deacetylase complex. J Biol Chem 277(17):14869-76 |
| abstractText | The multi-zinc finger proteins of the Sal family regulate organogenesis. Genetic evidence from Drosophila has shown that spalt (sal) can alter gene expression in a cell autonomous fashion, but Sal proteins have never been directly analyzed for their ability to activate or repress transcription. In this report, we show that a member of the Sal family, mouse Sall1, is a potent transcriptional repressor. When fused to a heterologous DNA-binding domain, Sall1 represses transcription of a luciferase reporter by over 100-fold. Expression of the N terminus alone is sufficient for dose-responsive repression that, as shown by deletion analysis, requires the extreme N-terminal amino acids of the protein. The N terminus of Sall1 can repress at both short and long range relative to the promoter, and treatment with the histone deacetylase (HDAC) inhibitor, trichostatin A, alleviates repression by 3-fold. The same regions of the protein that are required for repression physically interact with components of chromatin remodeling complexes, HDAC1, HDAC2, RbAp46/48, MTA-1, and MTA-2. Finally, we demonstrate that Sall1 is localized to discrete nuclear foci and this localization depends on the N-terminal repression domain. Together, these results suggest that the N terminus of mouse Sall1 can recruit HDAC complexes to mediate transcriptional repression. |
