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DExD/H 盒 ATP 酶 Dhh1 在翻译抑制、mRNA 衰变和处理体动力学中发挥作用。

The DExD/H box ATPase Dhh1 functions in translational repression, mRNA decay, and processing body dynamics.

机构信息

Department of Molecular and Cell Biology, Division of Cell and Developmental Biology, University of California, Berkeley, Berkeley, CA 94720, USA.

出版信息

J Cell Biol. 2011 Aug 22;194(4):527-37. doi: 10.1083/jcb.201007151. Epub 2011 Aug 15.

DOI:10.1083/jcb.201007151
PMID:21844211
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3160580/
Abstract

Translation, storage, and degradation of messenger ribonucleic acids (mRNAs) are key steps in the posttranscriptional control of gene expression, but how mRNAs transit between these processes remains poorly understood. In this paper, we functionally characterized the DExD/H box adenosine triphosphatase (ATPase) Dhh1, a critical regulator of the cytoplasmic fate of mRNAs. Using mRNA tethering experiments in yeast, we showed that Dhh1 was sufficient to move an mRNA from an active state to translational repression. In actively dividing cells, translational repression was followed by mRNA decay; however, deleting components of the 5'-3' decay pathway uncoupled these processes. Whereas Dhh1's ATPase activity was not required to induce translational inhibition and mRNA decay when directly tethered to an mRNA, ATP hydrolysis regulated processing body dynamics and the release of Dhh1 from these RNA-protein granules. Our results place Dhh1 at the interface of translation and decay controlling whether an mRNA is translated, stored, or decayed.

摘要

信使核糖核酸(mRNA)的翻译、储存和降解是基因表达转录后调控的关键步骤,但 mRNAs 在这些过程之间如何转移仍知之甚少。在本文中,我们从功能上对 DExD/H 盒腺苷三磷酸酶(ATP 酶) Dhh1 进行了表征,Dhh1 是 mRNA 细胞质命运的关键调节因子。通过在酵母中的 mRNA 系绳实验,我们表明 Dhh1 足以将 mRNA 从活跃状态转移到翻译抑制状态。在细胞分裂活跃的细胞中,翻译抑制随后是 mRNA 降解;然而,删除 5'-3' 降解途径的成分会使这些过程解耦。虽然当直接与 mRNA 系绳时,Dhh1 的 ATP 酶活性不需要诱导翻译抑制和 mRNA 降解,但 ATP 水解调节了处理体的动态,以及 Dhh1 从这些 RNA-蛋白质颗粒中的释放。我们的结果将 Dhh1 置于翻译和降解的界面,控制 mRNA 是翻译、储存还是降解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/18f3609ea1f0/JCB_201007151_RGB_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/9a70a1f825b4/JCB_201007151_GS_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/71fac91e3c7f/JCB_201007151_GS_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/c8c07aeb1162/JCB_201007151_RGB_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/7b3226dddd2a/JCB_201007151_GS_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/18f3609ea1f0/JCB_201007151_RGB_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/9a70a1f825b4/JCB_201007151_GS_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/71fac91e3c7f/JCB_201007151_GS_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/c8c07aeb1162/JCB_201007151_RGB_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/7b3226dddd2a/JCB_201007151_GS_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f481/3160580/18f3609ea1f0/JCB_201007151_RGB_Fig5.jpg

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