信使核糖核酸输出因子Mtr2和p15在缺乏序列同源性时的结构相似性。
Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15.
作者信息
Fribourg Sébastien, Conti Elena
机构信息
European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
出版信息
EMBO Rep. 2003 Jul;4(7):699-703. doi: 10.1038/sj.embor.embor883.
Abstract
The association between Mtr2 and Mex67 is essential for the nuclear export of bulk messenger RNA in yeast. In metazoans, the analogous function is carried out by the TAP-p15 heterodimer. Whereas Mex67 and TAP are highly conserved proteins, their binding partners, Mtr2 and p15, share no sequence similarity, but are nevertheless functionally homologous. Here, we report the 2.8-A resolution crystal structure of Mtr2 in complex with the NTF2-like domain of Mex67. Mtr2 is a novel member of the NTF2-like family and interacts with Mex67, forming a complex with a similar structural architecture to that of TAP-p15. Mtr2 fulfils an analogous function to that of human p15 in maintaining the structural integrity of the heterodimer. In addition, Mtr2 presents a long internal loop, which contains residues that affect the export of the large ribosomal subunit.
摘要
在酵母中，Mtr2与Mex67之间的关联对于大量信使核糖核酸的核输出至关重要。在后生动物中，类似功能由TAP-p15异二聚体执行。尽管Mex67和TAP是高度保守的蛋白质，但其结合伴侣Mtr2和p15没有序列相似性，但在功能上却是同源的。在此，我们报道了与Mex67的NTF2样结构域形成复合物的Mtr2的2.8埃分辨率晶体结构。Mtr2是NTF2样家族的一个新成员，与Mex67相互作用，形成一个与TAP-p15结构相似的复合物。Mtr2在维持异二聚体结构完整性方面发挥着与人类p15类似的功能。此外，Mtr2呈现出一个长的内部环，其中包含影响大核糖体亚基输出的残基。
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