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

J 2020

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

ROITHOVA, A., Zuzana FEKETOVÁ, Štěpánka VAŇÁČOVÁ a D. STANEK

Základní údaje

Originální název

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

Autoři

ROITHOVA, A., Zuzana FEKETOVÁ (703 Slovensko, domácí), Štěpánka VAŇÁČOVÁ (203 Česká republika, garant, domácí) a D. STANEK

Vydání

Nucleic acids research, Oxford, Oxford University Press, 2020, 0305-1048

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 16.971

Kód RIV

RIV/00216224:14740/20:00114751

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1093/nar/gkaa301

UT WoS

000574284500034

Klíčová slova anglicky

MESSENGER-RNA; DEGRADATION PATHWAY; NONCODING RNAS; TRANSLATION FACTORS; STRUCTURAL BASIS; TRUNCATED FORMS; QUALITY-CONTROL; CAJAL BODIES; CORE DOMAIN; COMPLEX

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 26. 2. 2021 12:30, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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.

Návaznosti

GA16-21341S, projekt VaV

Název: Studium úlohy uridylace RNA v lidských buňkách

Investor: Grantová agentura ČR, Studium úlohy uridylace RNA v lidských buňkách

GA20-19617S, projekt VaV

Název: Molekulární mechanismy nekanonických 3' terminálních modifikací RNA a jejich úloha v metabolismu kódujících a nekódujících RNA

Investor: Grantová agentura ČR, The molecular mechanisms of noncanonical 3' terminal RNA tailing and its role in the metabolism of coding and noncoding RNAs

LM2015062, projekt VaV

Název: Národní infrastruktura pro biologické a medicínské zobrazování

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, National research infrastructure for biological and medical imaging

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

ROITHOVA, A., Zuzana FEKETOVÁ, Štěpánka VAŇÁČOVÁ a D. STANEK. DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs. Nucleic acids research. Oxford: Oxford University Press, 2020, roč. 48, č. 11, s. 6184-6197. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkaa301.

@article{1746813,
   author = {Roithova, A. and Feketová, Zuzana and Vaňáčová, Štěpánka and Stanek, D.},
   article_location = {Oxford},
   article_number = {11},
   doi = {http://dx.doi.org/10.1093/nar/gkaa301},
   keywords = {MESSENGER-RNA; DEGRADATION PATHWAY; NONCODING RNAS; TRANSLATION FACTORS; STRUCTURAL BASIS; TRUNCATED FORMS; QUALITY-CONTROL; CAJAL BODIES; CORE DOMAIN; COMPLEX},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic acids research},
   title = {DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs},
   url = {https://academic.oup.com/nar/article/48/11/6184/5831191},
   volume = {48},
   year = {2020}
}

TY  - JOUR
ID  - 1746813
AU  - Roithova, A. - Feketová, Zuzana - Vaňáčová, Štěpánka - Stanek, D.
PY  - 2020
TI  - DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs
JF  - Nucleic acids research
VL  - 48
IS  - 11
SP  - 6184-6197
EP  - 6184-6197
PB  - Oxford University Press
SN  - 03051048
KW  - MESSENGER-RNA
KW  - DEGRADATION PATHWAY
KW  - NONCODING RNAS
KW  - TRANSLATION FACTORS
KW  - STRUCTURAL BASIS
KW  - TRUNCATED FORMS
KW  - QUALITY-CONTROL
KW  - CAJAL BODIES
KW  - CORE DOMAIN
KW  - COMPLEX
UR  - https://academic.oup.com/nar/article/48/11/6184/5831191
N2  - 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.
ER  -

ROITHOVA, A., Zuzana FEKETOVÁ, Štěpánka VAŇÁČOVÁ a D. STANEK. DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs. \textit{Nucleic acids research}. Oxford: Oxford University Press, 2020, roč.~48, č.~11, s.~6184-6197. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkaa301.

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