The crystal structure of nucleoplasmin-core: Implications for histone binding and nucleosome assembly

被引：140
|
作者：
Dutta, S
Akey, IV
Dingwall, C
Hartman, KL
Laue, T
Nolte, RT
Head, JF
Akey, CW
机构：
[1] Boston Univ, Sch Med, Dept Physiol & Biophys, Boston, MA 02118 USA
[2] GlaxoSmithKline, Neurobiol, CEDD, Harlow CM19 5AW, Essex, England
[3] Univ New Hampshire, Dept Biochem & Mol Biol, Durham, NH 03824 USA
[4] GlaxoSmithKline Res & Dev Ltd, Dept Struct Chem, Res Triangle Pk, NC 27709 USA
来源：
MOLECULAR CELL | 2001年 / 8卷 / 04期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1016/S1097-2765(01)00354-9
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：
The efficient assembly of histone complexes and nucleosomes requires the participation of molecular chaperones. Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 Angstrom resolution. The Np-core monomer is an eight-stranded beta barrel that fits snugly within a stable pentamer. In the crystal, two pentamers; associate to form a decamer. We show that both Np and Np-core are competent to assemble large complexes that contain the four core histones. Further experiments and modeling suggest that these complexes each contain five histone octamers; which dock to a central Np decamer. This work has important ramifications for models of histone storage, sperm chromatin decondensation, and nucleosome assembly.
引用
收藏
页码：841 / 853
页数：13
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