Pwp2 mediates UTP-B assembly via two structurally independent domains
العنوان: | Pwp2 mediates UTP-B assembly via two structurally independent domains |
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المؤلفون: | Boissier, F., Schmidt, C.M., Linnemann, J., Fribourg, S., Perez-Fernandez, J. |
المصدر: | Scientific Reports Scientific Reports, Vol 7, Iss 1, Pp 1-15 (2017) 'Scientific Reports ', vol: 7, pages: 3169-1-3169-15 (2017) |
سنة النشر: | 2017 |
مصطلحات موضوعية: | Protein Conformation, alpha-Helical, Ribosomal Proteins, Saccharomyces cerevisiae Proteins, Science, Gene Expression, Saccharomyces cerevisiae, Article, Gene Expression Regulation, Fungal, Escherichia coli, RNA Precursors, Protein Interaction Domains and Motifs, Cloning, Molecular, Phosphorylation, Binding Sites, Organelle Biogenesis, Nuclear Proteins, RNA-Binding Proteins, Recombinant Proteins, RNA, Ribosomal, Medicine, Protein Conformation, beta-Strand, Protein Multimerization, Ribosomes, Protein Binding |
الوصف: | 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. |
وصف الملف: | application/pdf |
تدمد: | 2045-2322 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::3f2ae3199467cf4d102e538b49ca1468 https://pubmed.ncbi.nlm.nih.gov/28600509 |
حقوق: | OPEN |
رقم الأكسشن: | edsair.pmid.dedup....3f2ae3199467cf4d102e538b49ca1468 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 20452322 |
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