Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes

Dimitar Angelov, Vladimir A. Bondarenko, Sébastien Almagro, Hervé Menoni, Fabien Mongélard, Fabienne Hans, Flore Mietton, Vasily M. Studitsky, Ali Hamiche, Stefan Dimitrov, Philippe Bouvet

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172 Citations (Scopus)


Remodeling machines play an essential role in the control of gene expression, but how their activity is regulated is not known. Here we report that the nuclear protein nucleolin possesses a histone chaperone activity and that this factor greatly enhances the activity of the chromatin remodeling machineries SWI/SNF and ACF. Interestingly, nucleolin is able to induce the remodeling by SWI/SNF of macroH2A, but not of H2ABbd nucleosomes, which are otherwise resistant to remodeling. This new histone chaperone promotes the destabilization of the histone octamer, helping the dissociation of a H2A-H2B dimer, and stimulates the SWI/SNF-mediated transfer of H2A-H2B dimers. Furthermore, nucleolin facilitates transcription through the nucleosome, which is reminiscent of the activity of the FACT complex. This work defines new functions for histone chaperones in chromatin remodeling and regulation of transcription and explains how nucleolin could act on transcription.

Original languageEnglish
Pages (from-to)1669-1679
Number of pages11
JournalEMBO Journal
Issue number8
Publication statusPublished - 19 Apr 2006
Externally publishedYes



  • macroH2A and H2ABbd histone variants
  • Nucleolin
  • Nucleosome
  • Remodeling
  • Transcription

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Angelov, D., Bondarenko, V. A., Almagro, S., Menoni, H., Mongélard, F., Hans, F., Mietton, F., Studitsky, V. M., Hamiche, A., Dimitrov, S., & Bouvet, P. (2006). Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes. EMBO Journal, 25(8), 1669-1679.