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Histone variant H2ABbd confers lower stability to the nucleosome.

Thierry Gautier 1, 2 D Wade Abbott 3 Annie Molla 4 Andre Verdel 1, 2 Juan Ausio 3, * Stefan Dimitrov 5, *
* Corresponding author
4 INSERM U823, équipe 4 (Chromatine et Epigénétique)
INSERM U823 - Institut d'oncologie/développement Albert Bonniot de Grenoble
5 INSERM U823, équipe 4 (Chromatine et Epigénétique)
Biologie moléculaire et cellulaire de la différenciation, INSERM U823 - Institut d'oncologie/développement Albert Bonniot de Grenoble
Abstract : The histone H2ABbd is a novel histone variant of H2A with a totally unknown function. We have investigated the behaviour of the H2ABbd nucleosomes. Nucleosomes were reconstituted with recombinant histone H2ABbd and changes in their conformations at different salt concentrations were studied by analytical centrifugation. The data are in agreement with H2ABbd being less tightly bound compared with conventional H2A in the nucleosome. In addition, stable cell lines expressing either green fluorescent protein (GFP)-H2A or GFP-H2ABbd were established and the mobility of both fusions was measured by fluorescence recovery after photobleaching. We show that GFP-H2ABbd exchanges much more rapidly than GFP-H2A within the nucleosome. The reported data are compatible with a lower stability of the variant H2ABbd nucleosome compared with the conventional H2A particle.
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Thierry Gautier, D Wade Abbott, Annie Molla, Andre Verdel, Juan Ausio, et al.. Histone variant H2ABbd confers lower stability to the nucleosome.. EMBO Reports, EMBO Press, 2004, 5 (7), pp.715-20. ⟨10.1038/sj.embor.7400182⟩. ⟨inserm-00335082⟩

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