Pwp2 mediates UTP-B assembly via two structurally independent domains

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 hier...

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Autores principales:	Fanny Boissier, Christina Maria Schmidt, Jan Linnemann, Sébastien Fribourg, Jorge Perez-Fernandez
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9fd30bdffdf942d49494977b2739e669
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spelling	oai:doaj.org-article:9fd30bdffdf942d49494977b2739e6692021-12-02T15:05:48ZPwp2 mediates UTP-B assembly via two structurally independent domains10.1038/s41598-017-03034-y2045-2322https://doaj.org/article/9fd30bdffdf942d49494977b2739e6692017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03034-yhttps://doaj.org/toc/2045-2322Abstract 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.Fanny BoissierChristina Maria SchmidtJan LinnemannSébastien FribourgJorge Perez-FernandezNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Fanny Boissier Christina Maria Schmidt Jan Linnemann Sébastien Fribourg Jorge Perez-Fernandez Pwp2 mediates UTP-B assembly via two structurally independent domains
description	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.
format	article
author	Fanny Boissier Christina Maria Schmidt Jan Linnemann Sébastien Fribourg Jorge Perez-Fernandez
author_facet	Fanny Boissier Christina Maria Schmidt Jan Linnemann Sébastien Fribourg Jorge Perez-Fernandez
author_sort	Fanny Boissier
title	Pwp2 mediates UTP-B assembly via two structurally independent domains
title_short	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_sort	pwp2 mediates utp-b assembly via two structurally independent domains
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/9fd30bdffdf942d49494977b2739e669
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_version_	1718388721444716544

Pwp2 mediates UTP-B assembly via two structurally independent domains

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