A Cascade of Histone Modifications Induces Chromatin Condensation in Mitosis

被引：194

作者：

Wilkins, Bryan J. ^{[1
]}

Rall, Nils A. ^{[1
]}

Ostwal, Yogesh ^{[2
]}

Kruitwagen, Tom ^{[3
]}

Hiragami-Hamada, Kyoko ^{[2
]}

Winkler, Marco ^{[1
]}

Barral, Yves ^{[3
]}

Fischle, Wolfgang ^{[2
]}

Neumann, Heinz ^{[1
]}

机构：

[1] Univ Gottingen, Inst Microbiol & Genet, Free Floater Jr Res Grp Appl Synthet Biol, D-37077 Gottingen, Germany

[2] Max Planck Inst Biophys Chem, Lab Chromatin Biochem, D-37077 Gottingen, Germany

[3] ETH, Inst Biochem, CH-8093 Zurich, Switzerland

来源：

SCIENCE | 2014年 / 343卷 / 6166期

基金：

欧洲研究理事会;

关键词：

GENETIC-CODE EXPANSION; CHROMOSOME COMPACTION; H4-K16; ACETYLATION; AURORA B; H3; PHOSPHORYLATION; CENTROMERE; KINASE; YEAST; ANAPHASE;

D O I：

10.1126/science.1244508

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.

引用

页码：77 / 80

页数：4

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