Histone variant H2ABbd confers lower stability to the nucleosome
Histone variant H2ABbd confers lower stability to the nucleosome
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DOI：
10.1038/sj.embor.7400182
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发表时间：
2004-07-01
期刊：
影响因子：
7.7
通讯作者：
Dimitrov, S
中科院分区：
文献类型：
--
作者：
Gautier, T;Abbott, DW;Dimitrov, S
组蛋白H2 ABbd是H2 A的一种新的组蛋白变体，其功能完全未知。我们研究了H2 ABbd核小体的行为。用重组组蛋白H2 ABbd重构核小体，并通过分析离心法研究其在不同盐浓度下的构象变化。这些数据与核小体中H2 ABbd与常规H2 A相比结合不那么紧密一致。此外，建立了表达绿色荧光蛋白（GFP）-H2 A或GFP-H2 ABbd的稳定细胞系，并通过光漂白后的荧光恢复来测量两种融合物的迁移率。我们表明，GFP-H2 ABbd交换更迅速地比GFP-H2 A内的核小体。所报道的数据与变体H2 ABbd核小体相比于常规H2 A颗粒的较低稳定性相容。
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.