The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway.
The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway.
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DOI：
10.1016/j.molcel.2010.08.021
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发表时间：
2010-09-24
期刊：
影响因子：
16
通讯作者：
Lorsch JR
中科院分区：
文献类型：
--
作者：
Mitchell SF;Walker SE;Algire MA;Park EH;Hinnebusch AG;Lorsch JR
翻译控制通常在mRNA募集到起始核糖体的阶段进行。我们用纯化的S.酿酒成分。我们发现eIF 3和eIF 4因子不仅稳定了mRNA与PIC的结合，还显著增加了募集速率。尽管加帽的mRNA需要eIF 3和eIF 4因子来有效募集到PIC，但在单独存在eIF 3的情况下可以募集未加帽的mRNA。帽强烈抑制这种替代募集途径，对eIF 4因子施加快速和稳定结合天然mRNA的要求。我们的数据表明，5′-帽在mRNA募集中既是一个积极的元件，也是一个消极的元件，在典型的mRNA处理因子组存在的情况下促进起始，同时阻止通过一个异常的、只需要eIF 3的替代途径与核糖体结合。
Translational control is frequently exerted at the stage of mRNA recruitment to the initiating ribosome. We have reconstituted mRNA recruitment to the 43S preinitiation complex (PIC) using purified S. cerevisiae components. We show that eIF3 and the eIF4 factors not only stabilize binding of mRNA to the PIC, they also dramatically increase the rate of recruitment. Although capped mRNAs require eIF3 and the eIF4 factors for efficient recruitment to the PIC, uncapped mRNAs can be recruited in the presence of eIF3 alone. The cap strongly inhibits this alternative recruitment pathway, imposing a requirement for the eIF4 factors for rapid and stable binding of natural mRNA. Our data suggest that the 5′-cap serves as both a positive and negative element in mRNA recruitment, promoting initiation in the presence of the canonical group of mRNA handling factors while preventing binding to the ribosome via an aberrant, alternative pathway requiring only eIF3.
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影响因子：
11.4
作者：
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