The Rtr1p CTD phosphatase autoregulates its mRNA through a degradation pathway involving the REX exonucleases.

The Rtr1p CTD phosphatase autoregulates its mRNA through a degradation pathway involving the REX exonucleases.
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RTR1P CTD磷酸酶通过涉及REX外切核酸酶的降解途径自动结合其mRNA。

DOI:
10.1261/rna.055723.115
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发表时间:
2016-04
期刊:
RNA (New York, N.Y.)
影响因子:
--
通讯作者:
Chanfreau G
Chanfreau G
中科院分区:
其他
文献类型:
--
作者:
Hodko D;Ward T;Chanfreau G

文献摘要

相似文献

Rtr 1 p是一种磷酸酶,通过调节RNA聚合酶II大亚基C端结构域的磷酸化状态来影响基因表达。在这里,我们表明,Rtr 1 p是一种新的mRNA降解途径,促进其自身的mRNA通过营业额的自动调节的组成部分。我们发现RTR 1 mRNA的3′UTR含有一个使该mRNA不稳定的顺式元件。RTR 1 mRNA周转是通过Rtr 1 p与RTR 1 mRNP的结合实现的,其方式依赖于该顺式元件。遗传证据表明,RTR 1 p介导的RTR 1 mRNA的降解涉及5′-3′ DExD/H-box RNA解旋酶Dhh 1 p和3′-5′外切核酸酶Rex 2 p和Rex 3 p。发现Rtr 1 p和Rex 3 p与Dhh 1 p相关,这表明了将雷克斯核酸外切酶募集到RTR 1 mRNA中进行降解的模型。RTR 1 p介导的衰变可能会影响其他转录物,包括未剪接的BMH 2前mRNA。我们建议,Rtr 1 p可能印记其RNA目标cotranscriptionally和确定其下游的降解机制,通过指导这些成绩单到一个新的营业额途径,涉及Rtr 1 p,Dhh 1 p,和雷克斯家族的核酸外切酶。
Rtr1p is a phosphatase that impacts gene expression by modulating the phosphorylation status of the C-terminal domain of the large subunit of RNA polymerase II. Here, we show that Rtr1p is a component of a novel mRNA degradation pathway that promotes its autoregulation through turnover of its own mRNA. We show that the 3′UTR of the RTR1 mRNA contains a cis element that destabilizes this mRNA. RTR1 mRNA turnover is achieved through binding of Rtr1p to the RTR1 mRNP in a manner that is dependent on this cis element. Genetic evidence shows that Rtr1p-mediated decay of the RTR1 mRNA involves the 5′-3′ DExD/H-box RNA helicase Dhh1p and the 3′-5′ exonucleases Rex2p and Rex3p. Rtr1p and Rex3p are found associated with Dhh1p, suggesting a model for recruiting the REX exonucleases to the RTR1 mRNA for degradation. Rtr1p-mediated decay potentially impacts additional transcripts, including the unspliced BMH2 pre-mRNA. We propose that Rtr1p may imprint its RNA targets cotranscriptionally and determine their downstream degradation mechanism by directing these transcripts to a novel turnover pathway that involves Rtr1p, Dhh1p, and the REX family of exonucleases.