Evidence map›Paper›PMID 20419091›Full record

ArticlePloS one2010

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

Andreas Neueder, Steffen Jakob, Gisela Pöll, Jan Linnemann, Rainer Deutzmann, Herbert Tschochner, Philipp Milkereit

Abstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

  1. Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function.International journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Andreas NeuederInstitut für Biochemie, Genetik und Mikrobiologie, University of Regensburg, Regensburg, Germany.
Steffen Jakob
Gisela Pöll
Jan Linnemann
Rainer Deutzmann
Herbert Tschochner
Philipp Milkereit

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Models, MolecularProtein TransportRibosomal ProteinsRibosome Subunits, SmallRNA, Ribosomal, 18SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionRibosomal Proteinsribosomal protein S5RNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID20419091
PMCPMC2856670

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.