Histone variant H2ABbd confers lower stability to the nucleosome

Thierry Gautier, D. Wade Abbott, Annie Molla, Andre Verdel, Juan Ausio, Stefan Dimitrov

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100 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)715-720
Number of pages6
JournalEMBO Reports
Volume5
Issue number7
DOIs
Publication statusPublished - Jul 2004
Externally publishedYes

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Keywords

  • Analytical centrifugation
  • FRAP
  • Histone variant H2ABbd
  • Nucleosomes
  • Stability

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Gautier, T., Abbott, D. W., Molla, A., Verdel, A., Ausio, J., & Dimitrov, S. (2004). Histone variant H2ABbd confers lower stability to the nucleosome. EMBO Reports, 5(7), 715-720. https://doi.org/10.1038/sj.embor.7400182