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Histone variant H2ABbd confers lower stability to the nucleosome
Author(s) -
Gautier Thierry,
Abbott D Wade,
Molla Annie,
Verdel Andre,
Ausio Juan,
Dimitrov Stefan
Publication year - 2004
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400182
Subject(s) - nucleosome , histone , green fluorescent protein , fluorescence recovery after photobleaching , biophysics , chromatin , photobleaching , chemistry , microbiology and biotechnology , biology , fluorescence , biochemistry , dna , physics , gene , optics , membrane
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.