Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense- mediated mRNA decay.
Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense- mediated mRNA decay.
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DOI：
10.1016/j.cell.2010.11.043
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发表时间：
2010-12-10
期刊：
影响因子：
64.5
通讯作者：
Lykke-Andersen J
中科院分区：
文献类型：
--
作者：
Franks TM;Singh G;Lykke-Andersen J
细胞mRNA存在于信使核糖核蛋白（mRNP）复合物中，其在mRNA的寿命期间经历转变并指导转录后基因调控。基因表达的最后一个转录后步骤是mRNP的周转，这涉及mRNA的降解和相关蛋白质的再循环。如何紧密相关的蛋白质组分是从降解mRNP释放是未知的。在这里，我们证明了RNA解旋酶Upf1的ATP酶活性允许进行无义介导的mRNA衰变（NMD）的mRNP的拆卸。在Upf 1 ATP酶活性的情况下，部分降解的NMD mRNA中间体与NMD因子复合物积累并集中在加工体中。因此，进行NMD的mRNP的分解和完成周转需要Upf 1的ATP水解。这揭示了mRNA衰变中一个以前未被认识和潜在调控的步骤，并提出了其他mRNA衰变途径如何释放底物mRNP的蛋白质组分的问题。
Cellular mRNAs exist in messenger ribonucleoprotein (mRNP) complexes, which undergo transitions during the lifetime of the mRNAs and direct posttranscriptional gene regulation. A final posttranscriptional step in gene expression is the turnover of the mRNP, which involves degradation of the mRNA and recycling of associated proteins. How tightly associated protein components are released from degrading mRNPs is unknown. Here we demonstrate that the ATPase activity of the RNA helicase Upf1 allows disassembly of mRNPs undergoing nonsense-mediated mRNA decay (NMD). In the absence of Upf1 ATPase activity, partially degraded NMD mRNA intermediates accumulate in complex with NMD factors and concentrate in processing bodies. Thus, disassembly and completion of turnover of mRNPs undergoing NMD requires ATP hydrolysis by Upf1. This uncovers a previously unappreciated and potentially regulated step in mRNA decay, and raises the question of how other mRNA decay pathways release protein components of substrate mRNPs.
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