Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro
Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro
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DOI：
10.1016/s1097-2765(00)80442-6
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发表时间：
2000-03-01
期刊：
影响因子：
16
通讯作者：
Wilusz, J
中科院分区：
文献类型：
--
作者：
Gao, M;Fritz, DT;Wilusz, J
我们已经使用了一个在体外系统，再现在体内方面的mRNA周转，以阐明去腺苷化的机制。DAN是负责体外poly（A）尾缩短的主要酶，其特异性地与RNA底物的5'帽结构相互作用，并且这种相互作用被poly（A）尾极大地刺激。一些观察结果表明，帽-DAN相互作用的调节mRNA的稳定性和翻译之间的网络功能是重要的。首先，未加帽的RNA底物是低效去腺苷化的。第二，5' UTR中的茎环结构通过干扰cap-DAN相互作用而显著降低去腺苷化。第三，帽结合蛋白eIF 4 E的添加在体外抑制去腺苷化。这些数据提供了对靶向mRNA降解的底物识别的早期步骤的见解。
We have used an in vitro system that reproduces in vivo aspects of mRNA turnover to elucidate mechanisms of deadenylation. DAN, the major enzyme responsible for poly(A) tail shortening in vitro, specifically interacts with the 5' cap structure of RNA substrates, and this interaction is greatly stimulated by a poly(A) tail. Several observations suggest that cap-DAN interactions are functionally important for the networking between regulated mRNA stability and translation. First, uncapped RNA substrates are inefficiently deadenylated. Second, a stem-loop structure in the 5' UTR dramatically reduces deadenylation by interfering with cap-DAN interactions. Third, the addition of cap binding protein eIF4E inhibits deadenylation in vitro. These data provide insights into the early steps of substrate recognition that target an mRNA for degradation.