Chromosomal protein HMGN1 modulates histone H3 phosphorylation

被引：111

作者：

Lim, JH ^{[1
]}

Catez, F ^{[1
]}

Birger, Y ^{[1
]}

West, KL ^{[1
]}

Prymakowska-Bosak, M ^{[1
]}

Postnikov, YV ^{[1
]}

Bustin, M ^{[1
]}

机构：

[1] NCI, Lab Metab, NIH, Bethesda, MD 20892 USA

来源：

MOLECULAR CELL | 2004年 / 15卷 / 04期

关键词：

D O I：

10.1016/j.molcel.2004.08.006

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：

Here we demonstrate that HMGN1, a nuclear protein that binds to nucleosomes and reduces the compaction of the chromatin fiber, modulates histone posttranslational modifications. In Hmgn1(-/-) cells, loss of HMGN1 elevates the steady-state levels,of phospho-S10-H3 and enhances the rate of stress-induced phosphorylation of S10-H3. In vitro, HMGN1 reduces the rate of phospho-S10-H3 by hindering the ability of kinases to modify nucleosomal, but not free, H3. During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin. We propose that the reduced binding of HMGN1 to nucleosomes, or the absence of the protein, improves access of anisomysin-induced kinases to H3. Thus, the levels of posttranslational modifications in chromatin are modulated by nucleosome binding proteins that alter the ability of enzymatic complexes to access and modify their nucleosomal targets.

引用

页码：573 / 584

页数：12

共 37 条

[1] THE FOOTPRINT OF CHROMOSOMAL-PROTEINS HMG-14 AND HMG-17 ON CHROMATIN SUBUNITS [J].