Boissier, Fanny and Schmidt, Christina Maria and Linnemann, Jan and Fribourg, Sebastien and Perez-Fernandez, Jorge (2017) Pwp2 mediates UTP-B assembly via two structurally independent domains. SCIENTIFIC REPORTS, 7: 3169. ISSN 2045-2322,
Full text not available from this repository. (Request a copy)Abstract
The SSU processome constitutes a large ribonucleoprotein complex involved in the early steps of ribosome biogenesis. UTP-B is one of the first multi-subunit protein complexes that associates with the pre-ribosomal RNA to form the SSU processome. To understand the molecular basis of the hierarchical assembly of the SSU-processome, we have undergone a structural and functional analysis of the UTP-B subunit Pwp2p. We show that Pwp2p is required for the proper assembly of UTP-B and for a productive association of UTP-B with pre-rRNA. These two functions are mediated by two distinct structural domains. The N-terminal domain of Pwp2p folds into a tandem WD-repeat (tWD) that associates with Utp21p, Utp18p, and Utp6p to form a core complex. The CTDs of Pwp2p and Utp21p mediate the assembly of the heterodimer Utp12p: Utp13p that is required for the stable incorporation of the UTP-B complex in the SSU processome. Finally, we provide evidence suggesting a role of UTP-B as a platform for the binding of assembly factors during the maturation of 20S rRNA precursors.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PRE-RIBOSOMAL-RNA; EUKARYOTIC RIBOSOME; SACCHAROMYCES-CEREVISIAE; U3 SNORNA; YEAST; PROTEINS; COMPLEX; TRANSCRIPTION; BIOGENESIS; VERSATILE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III > Prof. Dr. Herbert Tschochner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Dec 2018 13:10 |
| Last Modified: | 25 Feb 2019 12:54 |
| URI: | https://pred.uni-regensburg.de/id/eprint/704 |
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