人类核帽结合蛋白复合体与hnRNP F之间的相互作用
Interaction between the human nuclear cap-binding protein complex and hnRNP F.
作者信息
Gamberi C, Izaurralde E, Beisel C, Mattaj I W
机构信息
European Molecular Biology Laboratory, Heidelberg, Germany.
出版信息
Mol Cell Biol. 1997 May;17(5):2587-97. doi: 10.1128/MCB.17.5.2587.
Abstract
hnRNP F was identified in a screen for proteins that interact with human CBP80 and CBP20, the components of the nuclear cap-binding complex (CBC). In vitro interaction studies showed that hnRNP F can bind to both CBP20 and CBP80 individually. hnRNP F and CBC bind independently to RNA, but hnRNP F binds preferentially to CBC-RNA complexes rather than to naked RNA. The hnRNP H protein, which is 78% identical to hnRNP F and also interacts with both CBP80 and CBP20 in vitro, does not discriminate between naked RNA and CBC-RNA complexes, showing that this effect is specific. Depletion of hnRNP F from HeLa cell nuclear extract decreases the efficiency of pre-mRNA splicing, a defect which can be partially compensated by addition of recombinant hnRNP F. Thus, hnRNP F is required for efficient pre-mRNA splicing in vitro and may participate in the effect of CBC on pre-mRNA splicing.
摘要
在一项针对与人类CBP80和CBP20（核帽结合复合体（CBC）的组成成分）相互作用的蛋白质的筛选中，鉴定出了hnRNP F。体外相互作用研究表明，hnRNP F可分别与CBP20和CBP80结合。hnRNP F和CBC独立结合RNA，但hnRNP F优先结合CBC-RNA复合体而非裸露的RNA。hnRNP H蛋白与hnRNP F有78%的同源性，并且在体外也与CBP80和CBP20相互作用，但其对裸露RNA和CBC-RNA复合体并无区分，表明这种效应具有特异性。从HeLa细胞核提取物中去除hnRNP F会降低前体mRNA剪接的效率，添加重组hnRNP F可部分弥补这一缺陷。因此，hnRNP F是体外高效前体mRNA剪接所必需的，并且可能参与了CBC对前体mRNA剪接的影响。
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