Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain

被引：24

作者：

Ogawa, Y

Ono, T

Wakata, Y

Okawa, K

Tagami, H

Shibahara, K

机构：

[1] Natl Inst GEnet, Dept Integrated Genet, Mishima, Shizuoka 4118540, Japan

[2] Kyoto Univ, Grad Sch Med, HMRO, Biomol Characterizat Unit,Frontier Technol Ctr, Kyoto 6068501, Japan

[3] Nagoya Univ, Grad Sch Sci, Div Biol Sci, Chikusa Ku, Nagoya, Aichi 4648602, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 336卷 / 01期

基金：

日本学术振兴会; 日本科学技术振兴机构;

关键词：

histone macroH2A; histone variants; mono-ubiquitination; histone modification; facultative heterochromatin;

D O I：

10.1016/j.bbrc.2005.08.046

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：204 / 209

页数：6