U7小核核糖核蛋白颗粒（snRNP）独特的Sm核心结构：一种小核核糖核蛋白的深远意义
The special Sm core structure of the U7 snRNP: far-reaching significance of a small nuclear ribonucleoprotein.
作者信息
Schümperli D, Pillai R S
机构信息
Institute of Cell Biology, University of Bern, Baltzerstrasse 4, 3012, Bern, Switzerland.
出版信息
Cell Mol Life Sci. 2004 Oct;61(19-20):2560-70. doi: 10.1007/s00018-004-4190-0.
The polypeptide composition of the U7 small nuclear ribonucleoprotein (snRNP) involved in histone messenger RNA (mRNA) 3' end formation has recently been elucidated. In contrast to spliceosomal snRNPs, which contain a ring-shaped assembly of seven so-called Sm proteins, in the U7 snRNP the Sm proteins D1 and D2 are replaced by U7-specific Sm-like proteins, Lsm10 and Lsm11. This polypeptide composition and the unusual structure of Lsm11, which plays a role in histone RNA processing, represent new themes in the biology of Sm/Lsm proteins. Moreover this structure has important consequences for snRNP assembly that is mediated by two complexes containing the PRMT5 methyltransferase and the SMN (survival of motor neurons) protein, respectively. Finally, the ability to alter this polypeptide composition by a small mutation in U7 snRNA forms the basis for using modified U7 snRNA derivatives to alter specific pre-mRNA splicing events, thereby opening up a new way for antisense gene therapy.
参与组蛋白信使核糖核酸（mRNA）3'端形成的U7小核核糖核蛋白（snRNP）的多肽组成最近已被阐明。与包含七个所谓Sm蛋白的环形组装体的剪接体snRNP不同，在U7 snRNP中，Sm蛋白D1和D2被U7特异性Sm样蛋白Lsm10和Lsm11取代。这种多肽组成以及在组蛋白RNA加工中起作用的Lsm11的异常结构，代表了Sm/Lsm蛋白生物学中的新主题。此外，这种结构对分别由含有PRMT5甲基转移酶和SMN（运动神经元存活）蛋白的两个复合物介导的snRNP组装有重要影响。最后，通过U7 snRNA中的一个小突变改变这种多肽组成的能力，构成了使用修饰的U7 snRNA衍生物改变特定前体mRNA剪接事件的基础，从而为反义基因治疗开辟了一条新途径。
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