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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F20%3A00539703" target="_blank" >RIV/68378050:_____/20:00539703 - isvavai.cz</a>

Result on the web

<a href="https://academic.oup.com/nar/article/48/11/6184/5831191" target="_blank" >https://academic.oup.com/nar/article/48/11/6184/5831191</a>

DOI - Digital Object Identifier

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

Result language

angličtina

Original language name

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

Original language description

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' end and associate with DIS3L2 3'-> 5' exoribonuclease and LSm proteins. Finally, inhibition of 5'-> 3' 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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

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

Name of the periodical

Nucleic Acids Research

ISSN

1362-4962

e-ISSN

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Volume of the periodical

48

Issue of the periodical within the volume

11

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

6184-6197

UT code for WoS article

000574284500034

EID of the result in the Scopus database

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