![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
| Item Type: | Article |
|---|---|
| Title: | Common structural constituents confer IkappaB activity to NF-kappaB p105 and IkappaB/MAD-3 |
| Creators Name: | Hatada, E.N., Naumann, M. and Scheidereit, C. |
| Abstract: | The vertebrate NF-kappa B/c-rel inhibitors MAD-3/I kappa B alpha, I kappa B gamma/pdI and bcl-3 all share a conserved ankyrin repeat domain (ARD) consisting of six complete repeats, a short acidic motif and/or an incomplete seventh repeat. We present here a detailed analysis of the domain in p105/pdI and MAD-3/I kappa B involved in inhibition of DNA binding and in protein interaction with rel factors. We demonstrate that in both cases an acidic region and six ankyrin-like repeats are sufficient and required for protein interaction with the rel factors. However, for p105/pdI to achieve the high affinity needed to suppress DNA binding, an incomplete seventh repeat is required in addition. Both pdI and MAD-3 associate with rel proteins by forming heterotrimeric complexes, as shown by native gel analysis and by cross-linking. Furthermore, we demonstrate that deletion of only three amino acids in the first repeat converts the subunit specificity of the p105 ARD into that of MAD-3/I kappa B. We conclude that functionally the ARD in these molecules has a modular structure, with different subregions determining the specificity for the NF-kappa B subunits p50 and p65. |
| Keywords: | Ankyrin Repeats, Gene Expression, Nuclear Factor kappa B, Signal Transduction, Animals, Vertebrates |
| Source: | EMBO Journal |
| ISSN: | 0261-4189 |
| Publisher: | Oxford University Press |
| Volume: | 12 |
| Number: | 7 |
| Page Range: | 2781-2788 |
| Date: | July 1993 |
| Official Publication: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC413528/ |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
