RNA binding specificity of hnRNP proteins: a subset bind to the 3' end of introns.
RNA binding specificity of hnRNP proteins: a subset bind to the 3' end of introns.
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hnRNP 蛋白的 RNA 结合特异性：一个子集与内含子的 3 端结合。
DOI：
10.1002/j.1460-2075.1988.tb03228.x
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
Dreyfuss,G
中科院分区：
文献类型：
--
作者：
Swanson,MS;Dreyfuss,G
通过使用与RNase T1产生的片段结合的hnRNP蛋白的单克隆抗体免疫纯化，研究了hnRNP蛋白与核提取物中的前mRNA的结合，以及作为分离的蛋白。几种主要的hnRNP蛋白A1、C和D特异性结合内含子的3′端，该内含子位于分支位点和3′剪接位点之间含有保守的多聚嘧啶段的区域内。改变保守的3′剪接位点二核苷酸AG的突变会强烈削弱或消除A1蛋白以及抗Sm反应组分与该区域的结合。A1、C和D蛋白不能有效地结合细菌RNA或无内含子剪接产物（mRNA）的片段。这些蛋白质在内含子3′端的结合不需要加入外源性ATP提取物，但在加入ATP后仍然存在。这些发现表明，几种hnRNP蛋白对前mRNA具有RNA结合特异性，并提出了hnRNP颗粒结构和组装的模型。
The binding of hnRNP proteins to pre‐mRNAs in nuclear extracts, and as isolated proteins, was studied by using monoclonal antibody immunopurification of hnRNP proteins bound to RNase T1‐generated fragments. Several major hnRNP proteins, A1, C and D, bind specifically to the 3′ end of introns within a region containing the conserved polypyrimidine stretch between the branch site and the 3′ splice site. Mutations which alter the conserved 3′ splice site dinucleotide AG strongly impair or abolish the binding of the A1 protein as well as of an anti‐Sm reactive component(s) to this region. The A1, C and D proteins do not bind efficiently to fragments of either bacterial RNA or the intronless spliced product (mRNA). The binding of these proteins at the 3′ end of the intron does not require addition to the extract of exogenous ATP, but remains after ATP addition. These findings demonstrate that several hnRNP proteins have RNA binding specificities on pre‐mRNA, and suggest a model for hnRNP particle structure and assembly.