The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chrome domain dimer
The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chrome domain dimer
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DOI：
10.1093/emboj/19.7.1587
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发表时间：
2000-04-03
期刊：
影响因子：
11.4
通讯作者：
Laue, ED
中科院分区：
文献类型：
--
作者：
Brasher, SV;Smith, BO;Laue, ED
异染色质蛋白1 （HP1）家族蛋白通过形成异染色质结构参与基因沉默。它们由两个相关的结构域组成：n端铬结构域和c端阴影铬结构域。目前的结果表明，铬结构域可能作为蛋白质相互作用基序，将不同的蛋白质聚集在多蛋白复合物中，并将它们定位在异染色质中。我们之前已经从小鼠HP1 β蛋白MOD1中确定了铬结构域的结构，我们在这里表明，与铬结构域相反，阴影铬结构域是一个同二聚体。完整的HP1 β蛋白也是二聚体，其相互作用是由阴影铬结构域介导的，在柔性连接体的末端，铬结构域彼此独立移动。利用CAF1和TIF1 β蛋白片段进行的图谱研究表明，一个完整的二聚体阴影铬结构域结构是复杂形成所必需的。
The heterochromatin protein 1 (HP1) family of proteins is involved in gene silencing via the formation of heterochromatic structures. They are composed of two related domains: an N-terminal chrome domain and a C-terminal shadow chrome domain. Present results suggest that chrome domains may function as protein interaction motifs, bringing together different proteins in multi-protein complexes and locating them in heterochromatin, We have previously determined the structure of the chrome domain from the mouse HP1 beta protein, MOD1, We show here that, in contrast to the chrome domain, the shadow chrome domain is a homodimer. The intact HP1 beta protein is also dimeric, where the interaction is mediated by the shadow chrome domain, with the chrome domains moving independently of each other at the end of flexible linkers. Mapping studies, with fragments of the CAF1 and TIF1 beta proteins, show that an intact, dimeric, shadow chrome domain structure is required for complex formation.