Gautier Thierry, Abbott D Wade, Molla Annie, Verdel Andre, Ausio Juan, Dimitrov Stefan
Institut Albert Bonniot, INSERM U309, 38706 La Tronche cedex, France.
EMBO Rep. 2004 Jul;5(7):715-20. doi: 10.1038/sj.embor.7400182. Epub 2004 Jun 11.
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.
组蛋白H2ABbd是H2A的一种新型组蛋白变体,其功能完全未知。我们研究了H2ABbd核小体的行为。用重组组蛋白H2ABbd重构核小体,并通过分析离心研究其在不同盐浓度下的构象变化。数据表明,与核小体中的传统H2A相比,H2ABbd的结合较不紧密。此外,建立了表达绿色荧光蛋白(GFP)-H2A或GFP-H2ABbd的稳定细胞系,并通过光漂白后的荧光恢复测量了两种融合蛋白的迁移率。我们发现,在核小体中,GFP-H2ABbd的交换速度比GFP-H2A快得多。所报道的数据与变体H2ABbd核小体相比传统H2A颗粒稳定性较低相一致。