DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F20%3A10424177" target="_blank" >RIV/00216208:11310/20:10424177 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14740/20:00114751

Výsledek na webu

<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=aX9k84QGwb" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=aX9k84QGwb</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/nar/gkaa301" target="_blank" >10.1093/nar/gkaa301</a>

Jazyk výsledku

angličtina

Název v původním jazyce

DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs

Popis výsledku v původním jazyce

Spliceosomal small nuclear ribonucleoprotein particles (snRNPs) undergo a complex maturation pathway containing multiple steps in the nucleus and in the cytoplasm. snRNP biogenesis is strictly proof-read and several quality control checkpoints are placed along the pathway. Here, we analyzed the fate of small nuclear RNAs (snRNAs) that are unable to acquire a ring of Sm proteins. We showed that snRNAs lacking the Sm ring are unstable and accumulate in P-bodies in an LSm1-dependent manner. We further provide evidence that defective snRNAs without the Sm binding site are uridylated at the 3&apos; end and associate with DIS3L2 3&apos;-&gt; 5&apos; exoribonuclease and LSm proteins. Finally, inhibition of 5&apos;-&gt; 3&apos; exoribonuclease XRN1 increases association of Delta Sm snRNAs with DIS3L2, which indicates competition and compensation between these two degradation enzymes. Together, we provide evidence that defective snRNAs without the Sm ring are uridylated and degraded by alternative pathways involving either DIS3L2 or LSm proteins and XRN1.

Název v anglickém jazyce

DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs

Popis výsledku anglicky

Spliceosomal small nuclear ribonucleoprotein particles (snRNPs) undergo a complex maturation pathway containing multiple steps in the nucleus and in the cytoplasm. snRNP biogenesis is strictly proof-read and several quality control checkpoints are placed along the pathway. Here, we analyzed the fate of small nuclear RNAs (snRNAs) that are unable to acquire a ring of Sm proteins. We showed that snRNAs lacking the Sm ring are unstable and accumulate in P-bodies in an LSm1-dependent manner. We further provide evidence that defective snRNAs without the Sm binding site are uridylated at the 3&apos; end and associate with DIS3L2 3&apos;-&gt; 5&apos; exoribonuclease and LSm proteins. Finally, inhibition of 5&apos;-&gt; 3&apos; exoribonuclease XRN1 increases association of Delta Sm snRNAs with DIS3L2, which indicates competition and compensation between these two degradation enzymes. Together, we provide evidence that defective snRNAs without the Sm ring are uridylated and degraded by alternative pathways involving either DIS3L2 or LSm proteins and XRN1.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10600 - Biological sciences

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Nucleic Acids Research

ISSN

0305-1048

e-ISSN

—

Svazek periodika

48

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

14

Strana od-do

6184-6197

Kód UT WoS článku

000574284500034

EID výsledku v databázi Scopus

2-s2.0-85086524513