Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain
Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain
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DOI：
10.1016/j.bbrc.2005.08.046
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发表时间：
2005-10-14
影响因子：
3.1
通讯作者：
Shibahara, K
中科院分区：
文献类型：
--
作者：
Ogawa, Y;Ono, T;Shibahara, K
组蛋白 MacroH2A1.2 (macroH2A) 是一种不寻常的组蛋白 H2A 变体，在其羧基末端具有大型非组蛋白宏结构域。 MacroH2A1.2 富含兼性异染色质，包括雌性哺乳动物中失活的 X 染色体和衰老相关的异染色质灶。我们在此表明一小部分 MacroH2A1.2 在人类 HeLa 细胞中被单泛素化。质谱分析表明，单泛素化的具体靶位点是历史域的 Lysl 15 和 Lysl 16。组蛋白 H2A 中保守的相应 Lysl 19 也被多梳群复合物中的环蛋白单泛素化。我们认为，macroH2A1.2 和组蛋白 H2A 的单泛素化具有相似或协同作用，但 MacroH2A1.2 中的多个泛素化位点可能赋予 MacroH2A1.2 多种调节染色质状态的功能。 (c) 2005 Elsevier Inc. 保留所有权利。
Histone macroH2A1.2 (macroH2A) is an unusual histone H2A variant with a large non-histone macrodomain at its carboxyl terminal. MacroH2A1.2 is enriched in facultative heterochromatin, including inactivated X chromosomes in mammalian females and senescence-associated heterochromatin foci. We show here that a small population of macroH2A1.2 is mono-ubiquitinated in human HeLa cells. Mass spectrometry analysis revealed that the specific targeting sites for the mono-ubiquitination are Lysl 15 and Lysl 16 of the historic domain. A corresponding Lysl 19 conserved in histone H2A is also mono-ubiquitinated by Ring protein in the polycomb group complex. We suggest that the mono-ubiquitination of macroH2A1.2 and histone H2A has similar or synergistic implications, but that the multiple ubiquitination sites in macroH2A1.2 might confer a variety of functions upon macroH2A1.2 to modulate chromatin states. (c) 2005 Elsevier Inc. All rights reserved.