Centromere identity maintained by nucleosomes assembled with histone H3 containing the CENP-A targeting domain

被引：200

作者：

Black, Ben E. ^{[1
]}

Jansen, Lars E. T. ^{[1
]}

Maddox, Paul S. ^{[1
]}

Foltz, Daniel R. ^{[1
]}

Desai, Arshad B. ^{[1
]}

Shah, Jagesh V. ^{[1
]}

Cleveland, Don W. ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Cellular & Mol Med, La Jolla, CA 92093 USA

来源：

MOLECULAR CELL | 2007年 / 25卷 / 02期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/j.molcel.2006.12.018

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：

Active centromeres are marked by nucleosomes assembled with CENP-A, a centromere-specific histone H3 variant. The CENP-A centromere targeting domain (CATD), comprised of loop 1 and the alpha 2 helix within the histone fold, is sufficient to target histone H3 to centromeres and to generate the same conformational rigidity to the initial subnucleosomal heterotetramer with histone H4 as does CENP-A. We now show in human cells and in yeast that depletion of CENP-A is lethal, but recruitment of normal levels of kinetochore proteins, centromere-generated mitotic checkpoint signaling, chromosome segregation, and viability can be rescued by histone H3 carrying the CATD. These data offer direct support for centromere identity maintained by a unique nucleosome that serves to distinguish the centromere from the rest of the chromosome.

引用

页码：309 / 322

页数：14

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