由人类睾丸/精子特异性组蛋白H2B变体（hTSH2B）组成的核小体的表征。

Characterization of nucleosomes consisting of the human testis/sperm-specific histone H2B variant (hTSH2B).

作者信息

Li Andra, Maffey Allison H, Abbott Wade D, Conde e Silva Natalia, Prunell Ariel, Siino Joseph, Churikov Dmitrii, Zalensky Andrei O, Ausió Juan

机构信息

Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.

出版信息

Biochemistry. 2005 Feb 22;44(7):2529-35. doi: 10.1021/bi048061n.

DOI:10.1021/bi048061n

PMID:15709765

Abstract

We have reported earlier the occurrence of a specific histone H2B variant in human testis and sperm. Here we have structurally characterized this protein, its association with the rest of the histone octamer, and its effects on the nucleosome structure. We show that a reconstituted octamer consisting of hTSH2B and a stoichiometric complement of histones H2A, H3, and H4 exhibits a lower stability compared to the reconstituted native counterpart consisting of H2B. In contrast, the hTSH2B containing octamers are able to form nucleosome core particles which are structurally and dynamically indistinguishable from those reconstituted with octamers consisting of only native histones. Furthermore, the presence of hTSH2B in the nucleosome does not affect its ability to bind to linker histones.

摘要

我们之前曾报道过人睾丸和精子中存在一种特定的组蛋白H2B变体。在此，我们对该蛋白进行了结构表征，研究了其与组蛋白八聚体其他成分的关联，以及对核小体结构的影响。我们发现，由hTSH2B与组蛋白H2A、H3和H4的化学计量互补物组成的重组八聚体，与由H2B组成的重组天然八聚体相比，稳定性较低。相反，含有hTSH2B的八聚体能够形成核小体核心颗粒，其结构和动态特性与仅由天然组蛋白组成的八聚体重构的核小体核心颗粒无法区分。此外，核小体中hTSH2B的存在并不影响其与连接组蛋白结合的能力。