Structural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing
Structural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing
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Rtt106p 的结构分析揭示了异染色质沉默所需的 DNA 结合作用
DOI：
10.1074/jbc.m109.055996
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发表时间：
2010-02-05
影响因子：
4.8
通讯作者：
Shi, Yunyu
中科院分区：
文献类型：
--
作者：
Liu, Yiwei;Huang, Hongda;Shi, Yunyu
Rtt106p 是一种酿酒酵母组蛋白伴侣，在异染色质沉默和核小体组装中发挥作用。 Rtt106p 参与染色质动力学的分子机制仍不清楚。在这里，我们报道了 Rtt106p 核心结构域的 2.5 埃晶体结构，它采用了一种不寻常的“双普莱克斯特林同源性”结构域结构，代表了组蛋白伴侣的一种新颖的结构模式。已鉴定出组蛋白 H3-H4 结合区和新型双链 DNA 结合区。诱变研究表明，Rtt106p 的组蛋白和 DNA 结合活性参与 Sir 蛋白介导的异染色质形成。我们的结果揭示了 Rtt106p 多种功能的结构基础，并为其细胞作用提供了新的见解。
Rtt106p is a Saccharomyces cerevisiae histone chaperone with roles in heterochromatin silencing and nucleosome assembly. The molecular mechanism by which Rtt106p engages in chromatin dynamics remains unclear. Here, we report the 2.5 angstrom crystal structure of the core domain of Rtt106p, which adopts an unusual "double pleckstrin homology" domain architecture that represents a novel structural mode for histone chaperones. A histone H3-H4-binding region and a novel double-stranded DNA-binding region have been identified. Mutagenesis studies reveal that the histone and DNA binding activities of Rtt106p are involved in Sir protein-mediated heterochromatin formation. Our results uncover the structural basis of the diverse functions of Rtt106p and provide new insights into its cellular roles.