Chromosomal Protein HMGN1 Modulates the Phosphorylation of Serine 1 in Histone H2A
详细信息 查看全文
- 作者：Yuri V. Postnikov ; Galina I. Belova ; Jae-Hwan Lim ; Michael Bustin
- 刊名：Biochemistry
- 出版年：2006
- 出版时间：December 19, 2006
- 年：2006
- 卷：45
- 期：50
- 页码：15092 - 15099
- 全文大小：550K
- 年卷期：v.45,no.50(December 19, 2006)
- ISSN：1520-4995
文摘
Here we demonstrate that HMGN1, a nuclear protein that binds specifically to nucleosomes,modulates the level of histone H2A phosphorylation. In Hmgn1-/- cells, loss of HMGN1 elevates thesteady-state levels of H2AS1ph throughout the cell cycle. In vitro, HMGN1 reduces the rate of Rsk2- andMsk1-mediated phosphorylation of nucleosomal, but not free, histone H2A. HMGN1 inhibits H2Aphosphorylation by binding to nucleosomes since an HMGN mutant, which cannot bind to chromatin,does not inhibit the Rsk2- mediated H2A phosphorylation. HMGN2 also inhibits H2A phosphorylation,suggesting that the inhibition of H2A phosphorylation is not specific to only one member of this proteinfamily. Thus, the present data add modifications of histone H2A to the list of histone modifications affectedby HMGN proteins. It supports the suggestion that structural chromatin binding proteins can modify thewhole profile of post-translational modifications of core histones.