The histone octamer is invisible when NF-κB binds to the nucleosome

Dimitar Angelov, François Lenouvel, Fabienne Hans, Christoph W. Müller, Philippe Bouvet, Jan Bednar, Evangelos N. Moudrianakis, Jean Cadet, Stefan Dimitrov

Research output: Contribution to journalArticle

49 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)42374-42382
Number of pages9
JournalJournal of Biological Chemistry
Issue number41
Publication statusPublished - 8 Oct 2004


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Angelov, D., Lenouvel, F., Hans, F., Müller, C. W., Bouvet, P., Bednar, J., Moudrianakis, E. N., Cadet, J., & Dimitrov, S. (2004). The histone octamer is invisible when NF-κB binds to the nucleosome. Journal of Biological Chemistry, 279(41), 42374-42382.