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

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Abstract

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
Volume279
Issue number41
DOIs
Publication statusPublished - 8 Oct 2004
Externally publishedYes

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Nucleosomes
Histones
DNA
Transcription Factors
Genes
Switches

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Angelov, D., Lenouvel, F., Hans, F., Müller, C. W., Bouvet, P., Bednar, J., ... Dimitrov, S. (2004). The histone octamer is invisible when NF-κB binds to the nucleosome. Journal of Biological Chemistry, 279(41), 42374-42382. https://doi.org/10.1074/jbc.M407235200

The histone octamer is invisible when NF-κB binds to the nucleosome. / Angelov, Dimitar; Lenouvel, François; Hans, Fabienne; Müller, Christoph W.; Bouvet, Philippe; Bednar, Jan; Moudrianakis, Evangelos N.; Cadet, Jean; Dimitrov, Stefan.

In: Journal of Biological Chemistry, Vol. 279, No. 41, 08.10.2004, p. 42374-42382.

Research output: Contribution to journalArticle

Angelov, D, Lenouvel, F, Hans, F, Müller, CW, Bouvet, P, Bednar, J, Moudrianakis, EN, Cadet, J & Dimitrov, S 2004, 'The histone octamer is invisible when NF-κB binds to the nucleosome', Journal of Biological Chemistry, vol. 279, no. 41, pp. 42374-42382. https://doi.org/10.1074/jbc.M407235200
Angelov D, Lenouvel F, Hans F, Müller CW, Bouvet P, Bednar J et al. The histone octamer is invisible when NF-κB binds to the nucleosome. Journal of Biological Chemistry. 2004 Oct 8;279(41):42374-42382. https://doi.org/10.1074/jbc.M407235200
Angelov, Dimitar ; Lenouvel, François ; Hans, Fabienne ; Müller, Christoph W. ; Bouvet, Philippe ; Bednar, Jan ; Moudrianakis, Evangelos N. ; Cadet, Jean ; Dimitrov, Stefan. / The histone octamer is invisible when NF-κB binds to the nucleosome. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 41. pp. 42374-42382.
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