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. |
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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 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.
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