Article Dans Une Revue Journal of Biological Chemistry Année : 2004

The Histone Octamer Is Invisible When NF-κB Binds to the Nucleosome

Résumé

The transcription factor NF-κB is involved in the transcriptional control of more than 150 genes, but the way it acts at the level of nucleosomal templates is not known. Here we report on a study examining the interaction of NF-κB p50 with its DNA recognition sequence in a positioned nucleosome. We demonstrate that NF-κB p50 was able to bind to the nucleosome with an apparent association constant close to that for free DNA. In agreement with this, the affinity of NF-κB p50 binding does not depend on the localization of its recognition sequence relative to the nucleosome dyad axis. In addition, the binding of NF-κB p50 does not induce eviction of histones and does not perturb the overall structure of the nucleosome. The NF-κB p50-nucleosome complex exhibits, however, local structural alterations within the NF-κB p50 recognition site. Importantly, these alterations were very similar to those found in the NF-κB p50-DNA complex. Our data suggest that NF-κB p50 can accommodate the distorted, bent DNA within the nucleosome. This peculiar property of NF-κB p50 might have evolved to meet the requirements for its function as a central switch for stress responses
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hal-04906211 , version 1 (22-01-2025)

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Dimitar Angelov, François Lenouvel, Fabienne Hans, Christoph Müller, Philippe Bouvet, et al.. The Histone Octamer Is Invisible When NF-κB Binds to the Nucleosome. Journal of Biological Chemistry, 2004, 279 (41), pp.42374-42382. ⟨10.1074/jbc.M407235200⟩. ⟨hal-04906211⟩
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