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Common structural constituents confer IkappaB activity to NF-kappaB p105 and IkappaB/MAD-3

Item Type:Article
Title:Common structural constituents confer IkappaB activity to NF-kappaB p105 and IkappaB/MAD-3
Creators Name:Hatada, E.N. and 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:Nature Publishing Group (U.S.A.)
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

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