Structural elucidation of a PRP8 core domain from the heart of the spliceosome
Structural elucidation of a PRP8 core domain from the heart of the spliceosome
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DOI：
10.1038/nsmb.1505
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发表时间：
2008-11-01
影响因子：
16.8
通讯作者：
MacMillan, Andrew M.
中科院分区：
文献类型：
--
作者：
Ritchie, Dustin B.;Schellenberg, Matthew J.;MacMillan, Andrew M.
剪接体是一种复杂的核糖核蛋白 (RNP) 颗粒，含有 5 个 RNA 和 100 多种相关蛋白。其中一种蛋白质 PRP8 已被证明可直接与前体 mRNA (pre-mRNA) 和剪接体 RNA 的剪接位点和分支区域相互作用，并与剪接的两个步骤的催化相关。 PRP8 结构域 IV 核心的 1.85 埃 X 射线结构涉及关键的剪接体相互作用，揭示了二分结构，其中包括与五螺旋组装体相连的 RNase H 折叠的存在。对突变酵母等位基因和该结构背景下的交联结果的分析，再加上 RNA 结合研究，表明结构域 IV 形成了一个与剪接体催化核心处的 RNA 结构直接相互作用的表面。
The spliceosome is a complex ribonucleoprotein (RNP) particle containing five RNAs and more than 100 associated proteins. One of these proteins, PRP8, has been shown to interact directly with the splice sites and branch region of precursor-mRNAs (pre-mRNAs) and spliceosomal RNAs associated with catalysis of the two steps of splicing. The 1.85-angstrom X- ray structure of the core of PRP8 domain IV, implicated in key spliceosomal interactions, reveals a bipartite structure that includes the presence of an RNase H fold linked to a five-helix assembly. Analysis of mutant yeast alleles and cross-linking results in the context of this structure, coupled with RNA binding studies, suggests that domain IV forms a surface that interacts directly with the RNA structures at the catalytic core of the spliceosome.