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Pwp2 mediates UTP-B assembly via two structurally independent domains
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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5466602/ https://www.ncbi.nlm.nih.gov/pubmed/28600509 http://dx.doi.org/10.1038/s41598-017-03034-y |
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author | Boissier, Fanny Schmidt, Christina Maria Linnemann, Jan Fribourg, Sébastien Perez-Fernandez, Jorge |
author_facet | Boissier, Fanny Schmidt, Christina Maria Linnemann, Jan Fribourg, Sébastien Perez-Fernandez, Jorge |
author_sort | Boissier, Fanny |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5466602 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-54666022017-06-14 Pwp2 mediates UTP-B assembly via two structurally independent domains Boissier, Fanny Schmidt, Christina Maria Linnemann, Jan Fribourg, Sébastien Perez-Fernandez, Jorge Sci Rep Article 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. Nature Publishing Group UK 2017-06-09 /pmc/articles/PMC5466602/ /pubmed/28600509 http://dx.doi.org/10.1038/s41598-017-03034-y Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Boissier, Fanny Schmidt, Christina Maria Linnemann, Jan Fribourg, Sébastien Perez-Fernandez, Jorge Pwp2 mediates UTP-B assembly via two structurally independent domains |
title | Pwp2 mediates UTP-B assembly via two structurally independent domains |
title_full | Pwp2 mediates UTP-B assembly via two structurally independent domains |
title_fullStr | Pwp2 mediates UTP-B assembly via two structurally independent domains |
title_full_unstemmed | Pwp2 mediates UTP-B assembly via two structurally independent domains |
title_short | Pwp2 mediates UTP-B assembly via two structurally independent domains |
title_sort | pwp2 mediates utp-b assembly via two structurally independent domains |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5466602/ https://www.ncbi.nlm.nih.gov/pubmed/28600509 http://dx.doi.org/10.1038/s41598-017-03034-y |
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