PROTEIN-COMPONENTS SPECIFICALLY ASSOCIATED WITH PRESPLICEOSOME AND SPLICEOSOME COMPLEXES
PROTEIN-COMPONENTS SPECIFICALLY ASSOCIATED WITH PRESPLICEOSOME AND SPLICEOSOME COMPLEXES
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DOI：
10.1101/gad.6.10.1986
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发表时间：
1992-10-01
影响因子：
10.5
通讯作者：
REED, R
中科院分区：
文献类型：
--
作者：
BENNETT, M;MICHAUD, S;REED, R
我们对高纯度哺乳动物剪接体的蛋白质组成进行了系统的分析。我们发现，超过30种不同的蛋白质，包括20种以前未鉴定的组分[指定的剪接体相关蛋白（SAP）]，与抗盐复合物中的剪接体特异性相关。与这些剪接体特异性蛋白相比，我们发现hnRNP蛋白与纯化的前剪接体和剪接体复合物并不紧密相关。剪接因子U2AF65、U1 snRNP特异性蛋白和几种SAP存在于最早的前剪接体复合物中（E）。然后将一组10种蛋白质加入第一个ATP依赖性前剪接体复合物（A）中，同时观察到U2AF 65水平的显著降低。完全组装的剪接体通过在需要ATP和5'和3'剪接位点的反应中添加12种蛋白质形成。
We have carried out a systematic analysis of the protein composition of highly purified mammalian spliceosomes. We show that >30 distinct proteins, including 20 previously unidentified components [designated spliceosome-associated proteins (SAPs)], are specifically associated with the spliceosome in a salt-resistant complex. In contrast to these spliceosome-specific proteins, we show that hnRNP proteins are not tightly associated with purified prespliceosome and spliceosome complexes. The splicing factor U2AF65, U1 snRNP-specific proteins, and several SAPs are present in the earliest prespliceosome complex (E). A set of 10 proteins is then added to the first ATP-dependent prespliceosome complex (A), and concomitantly, a significant decrease in the level of U2AF65 is observed. The fully assembled spliceosome is formed by the addition of 12 proteins in a reaction that requires ATP and both the 5' and 3' splice sites.