| 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. |
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@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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