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 and D. STANEK

Basic information

Original name

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

Authors

ROITHOVA, A., Zuzana FEKETOVÁ (703 Slovakia, belonging to the institution), Štěpánka VAŇÁČOVÁ (203 Czech Republic, guarantor, belonging to the institution) and D. STANEK

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 16.971

RIV identification code

RIV/00216224:14740/20:00114751

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000574284500034

Keywords in English

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

Abstract

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.

Links

GA16-21341S, research and development project

Name: Studium úlohy uridylace RNA v lidských buňkách

Investor: Czech Science Foundation

GA20-19617S, research and development project

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

Investor: Czech Science Foundation

LM2015062, research and development project

Name: Národní infrastruktura pro biologické a medicínské zobrazování

Investor: Ministry of Education, Youth and Sports of the CR

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

ROITHOVA, A., Zuzana FEKETOVÁ, Štěpánka VAŇÁČOVÁ and D. STANEK. DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs. Nucleic acids research. Oxford: Oxford University Press, 2020, vol. 48, No 11, p. 6184-6197. ISSN 0305-1048. Available from: 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 and 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, vol.~48, No~11, p.~6184-6197. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkaa301.

Detailed Information on Publication Record