Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome

Cécile Marie Doyen, Fabien Montel, Thierry Gautier, Hervé Menoni, Cyril Claudet, Marlène Delacour-Larose, Dimitri Angelov, Ali Hamiche, Jan Bednar, Cendrine Faivre-Moskalenko, Philippe Bouvet, Stefan Dimitrov

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

The histone variant H2A.Bbd appeared to be associated with active chromatin, but how it functions is unknown. We have dissected the properties of nucleosome containing H2A.Bbd. Atomic force microscopy (AFM) and electron cryo-microscopy (cryo-EM) showed that the H2A.Bbd histone octamer organizes only ∼130 bp of DNA, suggesting that 10 bp of each end of nucleosomal DNA are released from the octamer. In agreement with this, the entry/exit angle of the nucleosomal DNA ends formed an angle close to 180° and the physico-chemical analysis pointed to a lower stability of the variant particle. Reconstitution of nucleosomes with swapped-tail mutants demonstrated that the N-terminus of H2A.Bbd has no impact on the nucleosome properties. AFM, cryo-EM and chromatin remodeling experiments showed that the overall structure and stability of the particle, but not its property to interfere with the SWI/SNF induced remodeling, were determined to a considerable extent by the H2A.Bbd docking domain. These data show that the whole H2A.Bbd histone fold domain is responsible for the unusual properties of the H2A.Bbd nucleosome.

Original languageEnglish
Pages (from-to)4234-4244
Number of pages11
JournalEMBO Journal
Volume25
Issue number18
DOIs
Publication statusPublished - 20 Sep 2006
Externally publishedYes

Fingerprint

Dissection
Nucleosomes
Histones
Atomic Force Microscopy
Chromatin
Atomic force microscopy
DNA
Cryoelectron Microscopy
Chromatin Assembly and Disassembly
Microscopic examination
Electrons
Chemical analysis
Experiments

Keywords

  • Chromatin
  • H2A.Bbd
  • Histone variant
  • Nucleosome remodeling
  • Nucleosome stability

ASJC Scopus subject areas

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

Cite this

Doyen, C. M., Montel, F., Gautier, T., Menoni, H., Claudet, C., Delacour-Larose, M., ... Dimitrov, S. (2006). Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome. EMBO Journal, 25(18), 4234-4244. https://doi.org/10.1038/sj.emboj.7601310

Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome. / Doyen, Cécile Marie; Montel, Fabien; Gautier, Thierry; Menoni, Hervé; Claudet, Cyril; Delacour-Larose, Marlène; Angelov, Dimitri; Hamiche, Ali; Bednar, Jan; Faivre-Moskalenko, Cendrine; Bouvet, Philippe; Dimitrov, Stefan.

In: EMBO Journal, Vol. 25, No. 18, 20.09.2006, p. 4234-4244.

Research output: Contribution to journalArticle

Doyen, CM, Montel, F, Gautier, T, Menoni, H, Claudet, C, Delacour-Larose, M, Angelov, D, Hamiche, A, Bednar, J, Faivre-Moskalenko, C, Bouvet, P & Dimitrov, S 2006, 'Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome', EMBO Journal, vol. 25, no. 18, pp. 4234-4244. https://doi.org/10.1038/sj.emboj.7601310
Doyen CM, Montel F, Gautier T, Menoni H, Claudet C, Delacour-Larose M et al. Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome. EMBO Journal. 2006 Sep 20;25(18):4234-4244. https://doi.org/10.1038/sj.emboj.7601310
Doyen, Cécile Marie ; Montel, Fabien ; Gautier, Thierry ; Menoni, Hervé ; Claudet, Cyril ; Delacour-Larose, Marlène ; Angelov, Dimitri ; Hamiche, Ali ; Bednar, Jan ; Faivre-Moskalenko, Cendrine ; Bouvet, Philippe ; Dimitrov, Stefan. / Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome. In: EMBO Journal. 2006 ; Vol. 25, No. 18. pp. 4234-4244.
@article{caa5c00692ff40b2b4af1e53560ed07c,
title = "Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome",
abstract = "The histone variant H2A.Bbd appeared to be associated with active chromatin, but how it functions is unknown. We have dissected the properties of nucleosome containing H2A.Bbd. Atomic force microscopy (AFM) and electron cryo-microscopy (cryo-EM) showed that the H2A.Bbd histone octamer organizes only ∼130 bp of DNA, suggesting that 10 bp of each end of nucleosomal DNA are released from the octamer. In agreement with this, the entry/exit angle of the nucleosomal DNA ends formed an angle close to 180° and the physico-chemical analysis pointed to a lower stability of the variant particle. Reconstitution of nucleosomes with swapped-tail mutants demonstrated that the N-terminus of H2A.Bbd has no impact on the nucleosome properties. AFM, cryo-EM and chromatin remodeling experiments showed that the overall structure and stability of the particle, but not its property to interfere with the SWI/SNF induced remodeling, were determined to a considerable extent by the H2A.Bbd docking domain. These data show that the whole H2A.Bbd histone fold domain is responsible for the unusual properties of the H2A.Bbd nucleosome.",
keywords = "Chromatin, H2A.Bbd, Histone variant, Nucleosome remodeling, Nucleosome stability",
author = "Doyen, {C{\'e}cile Marie} and Fabien Montel and Thierry Gautier and Herv{\'e} Menoni and Cyril Claudet and Marl{\`e}ne Delacour-Larose and Dimitri Angelov and Ali Hamiche and Jan Bednar and Cendrine Faivre-Moskalenko and Philippe Bouvet and Stefan Dimitrov",
year = "2006",
month = "9",
day = "20",
doi = "10.1038/sj.emboj.7601310",
language = "English",
volume = "25",
pages = "4234--4244",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "18",

}

TY - JOUR

T1 - Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome

AU - Doyen, Cécile Marie

AU - Montel, Fabien

AU - Gautier, Thierry

AU - Menoni, Hervé

AU - Claudet, Cyril

AU - Delacour-Larose, Marlène

AU - Angelov, Dimitri

AU - Hamiche, Ali

AU - Bednar, Jan

AU - Faivre-Moskalenko, Cendrine

AU - Bouvet, Philippe

AU - Dimitrov, Stefan

PY - 2006/9/20

Y1 - 2006/9/20

N2 - The histone variant H2A.Bbd appeared to be associated with active chromatin, but how it functions is unknown. We have dissected the properties of nucleosome containing H2A.Bbd. Atomic force microscopy (AFM) and electron cryo-microscopy (cryo-EM) showed that the H2A.Bbd histone octamer organizes only ∼130 bp of DNA, suggesting that 10 bp of each end of nucleosomal DNA are released from the octamer. In agreement with this, the entry/exit angle of the nucleosomal DNA ends formed an angle close to 180° and the physico-chemical analysis pointed to a lower stability of the variant particle. Reconstitution of nucleosomes with swapped-tail mutants demonstrated that the N-terminus of H2A.Bbd has no impact on the nucleosome properties. AFM, cryo-EM and chromatin remodeling experiments showed that the overall structure and stability of the particle, but not its property to interfere with the SWI/SNF induced remodeling, were determined to a considerable extent by the H2A.Bbd docking domain. These data show that the whole H2A.Bbd histone fold domain is responsible for the unusual properties of the H2A.Bbd nucleosome.

AB - The histone variant H2A.Bbd appeared to be associated with active chromatin, but how it functions is unknown. We have dissected the properties of nucleosome containing H2A.Bbd. Atomic force microscopy (AFM) and electron cryo-microscopy (cryo-EM) showed that the H2A.Bbd histone octamer organizes only ∼130 bp of DNA, suggesting that 10 bp of each end of nucleosomal DNA are released from the octamer. In agreement with this, the entry/exit angle of the nucleosomal DNA ends formed an angle close to 180° and the physico-chemical analysis pointed to a lower stability of the variant particle. Reconstitution of nucleosomes with swapped-tail mutants demonstrated that the N-terminus of H2A.Bbd has no impact on the nucleosome properties. AFM, cryo-EM and chromatin remodeling experiments showed that the overall structure and stability of the particle, but not its property to interfere with the SWI/SNF induced remodeling, were determined to a considerable extent by the H2A.Bbd docking domain. These data show that the whole H2A.Bbd histone fold domain is responsible for the unusual properties of the H2A.Bbd nucleosome.

KW - Chromatin

KW - H2A.Bbd

KW - Histone variant

KW - Nucleosome remodeling

KW - Nucleosome stability

UR - http://www.scopus.com/inward/record.url?scp=33748931801&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33748931801&partnerID=8YFLogxK

U2 - 10.1038/sj.emboj.7601310

DO - 10.1038/sj.emboj.7601310

M3 - Article

VL - 25

SP - 4234

EP - 4244

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 18

ER -