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A role for DIS3L2 over natural nonsense-mediated mRNA decay targets in human cells.

Abstract：

:The nonsense-mediated decay (NMD) pathway selectively degrades mRNAs carrying a premature translation-termination codon but also regulates the abundance of a large number of physiological mRNAs that encode full-length proteins. In human cells, NMD-targeted mRNAs are degraded by endonucleolytic cleavage and exonucleolytic degradation from both 5-' and 3'-ends. This is done by a process not yet completely understood that recruits decapping and 5'-to-3' exonuclease activities, as well as deadenylating and 3'-to-5' exonuclease exosome activities. In yeast, DIS3/Rrp44 protein is the catalytic subunit of the exosome, but in humans, there are three known paralogues of this enzyme: DIS3, DIS3L1, and DIS3L2. However, little is known about their role in NMD. Here, we show that some NMD-targets are DIS3L2 substrates in human cells. In addition, we observed that DIS3L2 acts over full-length transcripts, through a process that also involves UPF1. Moreover, DIS3L2-mediated decay is dependent on the activity of the terminal uridylyl transferases Zcchc6/11 (TUT7/4). Together, our findings establish a role for DIS3L2 and uridylation in NMD.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

da Costa PJ,Menezes J,Saramago M,García-Moreno JF,Santos HA,Gama-Carvalho M,Arraiano CM,Viegas SC,Romão L

doi

10.1016/j.bbrc.2019.08.105

subject

Has Abstract

pub_date

2019-10-22 00:00:00

pages

664-671

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)31628-6

journal_volume

518

pub_type

杂志文章

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