Interaction between the human nuclear cap-binding protein complex and hnRNP F
Interaction between the human nuclear cap-binding protein complex and hnRNP F
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DOI：
10.1128/mcb.17.5.2587
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发表时间：
1997-05-01
影响因子：
5.3
通讯作者：
Mattaj, IW
中科院分区：
文献类型：
--
作者：
Gamberi, C;Izaurralde, E;Mattaj, IW
hnRNP F是在筛选与人CBP 80和CBP 20（核帽结合复合物（CBC）的组分）相互作用的蛋白质中鉴定的。体外相互作用研究表明，hnRNP F可以分别与CBP 20和CBP 80结合。hnRNP F和CBC独立地结合RNA，但hnRNP F优先结合CBC-RNA复合物而不是裸RNA。hnRNP H蛋白与hnRNP F具有78%的同一性，并且在体外也与CBP 80和CBP 20相互作用，其不区分裸RNA和CBC-RNA复合物，表明这种作用是特异性的。HeLa细胞核提取物中hnRNP F的消耗降低了前mRNA剪接的效率，这种缺陷可以通过加入重组hnRNP F来部分补偿。因此，hnRNP F是体外有效的前体mRNA剪接所必需的，并且可能参与CBC对前体mRNA剪接的影响。
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.