A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.

In vivo depletion of the yeast small ribosomal subunit (SSU) protein S5 (rpS5) leads to nuclear degradation of nascent SSUs and to a perturbed global assembly state of the SSU head domain. Here, we report that rpS5 plays an additional local role at the head/platform interface in efficient SSU matura...

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Autores principales:	Andreas Neueder, Steffen Jakob, Gisela Pöll, Jan Linnemann, Rainer Deutzmann, Herbert Tschochner, Philipp Milkereit
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/672961b4494045cea66ce7d98d3f6711
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spelling	oai:doaj.org-article:672961b4494045cea66ce7d98d3f67112021-11-25T06:24:29ZA local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.1932-620310.1371/journal.pone.0010194https://doaj.org/article/672961b4494045cea66ce7d98d3f67112010-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20419091/?tool=EBIhttps://doaj.org/toc/1932-6203In vivo depletion of the yeast small ribosomal subunit (SSU) protein S5 (rpS5) leads to nuclear degradation of nascent SSUs and to a perturbed global assembly state of the SSU head domain. Here, we report that rpS5 plays an additional local role at the head/platform interface in efficient SSU maturation. We find that yeast small ribosomal subunits which incorporated an rpS5 variant lacking the seven C-terminal amino acids have a largely assembled head domain and are exported to the cytoplasm. On the other hand, 3' processing of 18S rRNA precursors is inhibited in these ribosomal particles, although they associate with the putative endonuclease Nob1p and other late acting 40S biogenesis factors. We suggest that the SSU head component rpS5 and platform components as rpS14 are crucial constituents of a highly defined spatial arrangement in the head-platform interface of nascent SSUs, which is required for efficient processing of the therein predicted SSU rRNA 3' end. Positioning of rpS5 in nascent SSUs, including its relative orientation towards platform components in the head-platform cleft, will depend on the general assembly and folding state of the head domain. Therefore, the suggested model can explain 18S precursor rRNA 3' processing phenotypes observed in many eukaryotic SSU head assembly mutants.Andreas NeuederSteffen JakobGisela PöllJan LinnemannRainer DeutzmannHerbert TschochnerPhilipp MilkereitPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 4, p e10194 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Andreas Neueder Steffen Jakob Gisela Pöll Jan Linnemann Rainer Deutzmann Herbert Tschochner Philipp Milkereit A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.
description	In vivo depletion of the yeast small ribosomal subunit (SSU) protein S5 (rpS5) leads to nuclear degradation of nascent SSUs and to a perturbed global assembly state of the SSU head domain. Here, we report that rpS5 plays an additional local role at the head/platform interface in efficient SSU maturation. We find that yeast small ribosomal subunits which incorporated an rpS5 variant lacking the seven C-terminal amino acids have a largely assembled head domain and are exported to the cytoplasm. On the other hand, 3' processing of 18S rRNA precursors is inhibited in these ribosomal particles, although they associate with the putative endonuclease Nob1p and other late acting 40S biogenesis factors. We suggest that the SSU head component rpS5 and platform components as rpS14 are crucial constituents of a highly defined spatial arrangement in the head-platform interface of nascent SSUs, which is required for efficient processing of the therein predicted SSU rRNA 3' end. Positioning of rpS5 in nascent SSUs, including its relative orientation towards platform components in the head-platform cleft, will depend on the general assembly and folding state of the head domain. Therefore, the suggested model can explain 18S precursor rRNA 3' processing phenotypes observed in many eukaryotic SSU head assembly mutants.
format	article
author	Andreas Neueder Steffen Jakob Gisela Pöll Jan Linnemann Rainer Deutzmann Herbert Tschochner Philipp Milkereit
author_facet	Andreas Neueder Steffen Jakob Gisela Pöll Jan Linnemann Rainer Deutzmann Herbert Tschochner Philipp Milkereit
author_sort	Andreas Neueder
title	A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.
title_short	A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.
title_full	A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.
title_fullStr	A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.
title_full_unstemmed	A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.
title_sort	local role for the small ribosomal subunit primary binder rps5 in final 18s rrna processing in yeast.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/672961b4494045cea66ce7d98d3f6711
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A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.

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