Self-association of trimethylguanosine synthase Tgs1 is required for efficient snRNA/snoRNA trimethylation and pre-rRNA processing
Trimethylguanosine Synthase catalyses transfer of two methyl groups to the m7G cap of RNA polymerase II transcribed snRNAs, snoRNAs and telomerase RNA TLC1 to form a 2,2,7-trimethylguanosine cap. While in vitro studies indicate that Tgs1 functions as a monomer and the dimethylation of m7G caps is no...
Gespeichert in:
| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
15 June 2015
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| In: |
Scientific reports
Year: 2015, Jahrgang: 5 |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep11282 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/srep11282 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/srep11282 
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| Verfasserangaben: | Kum-Loong Boon, Michael David Pearson & Martin Koš |
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| 520 | |a Trimethylguanosine Synthase catalyses transfer of two methyl groups to the m7G cap of RNA polymerase II transcribed snRNAs, snoRNAs and telomerase RNA TLC1 to form a 2,2,7-trimethylguanosine cap. While in vitro studies indicate that Tgs1 functions as a monomer and the dimethylation of m7G caps is not a processive reaction, partially methylated sn(o)RNAs are typically not detected in living cells. Here we show that both yeast and human Tgs1p possess a conserved self-association property located at the N-terminus. A disruption of Tgs1 self-association led to a strong reduction of sn(o)RNA trimethylation as well as reduced nucleolar enrichment of Tgs1. Self-association of Tgs1p and its catalytic activity were also prerequisite to bypass the requirement for its accessory factor Swm2p for efficient pre-rRNA processing and snRNA trimethylation. The ability to self-associate might enable Tgs1 to efficiently dimethylate the caps of the targeted RNAs in vivo. | ||
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