Evidence map›Paper›PMID 22688513›Full record

ArticleMolecular and cellular biology2012

Saccharomyces cerevisiae ribosomal protein L26 is not essential for ribosome assembly and function.

Reyes Babiano, Michael Gamalinda, John L Woolford, Jesús de la Cruz

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 59 citations in OpenAlex.

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  12. Ribosomal protein RPL26 is the principal target of UFMylation.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

4 authors at 2 institutions in 2 countries.

Reyes BabianoDepartamento de Genética, Universidad de Sevilla, Seville, Spain.
Michael Gamalinda
John L Woolford
Jesús de la Cruz
Carnegie Mellon University · USUniversidad de Sevilla · ES

Funding

YEAST RIBOSOME BIOGENESISR01GM028301 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WOOLFORD, JOHN L. · 1985 to 2025
$8.4M
NIGMS NIH HHS R01 GM028301
6 · The paper itself

Abstract

Ribosomal proteins play important roles in ribosome biogenesis and function. Here, we study the evolutionarily conserved L26 in Saccharomyces cerevisiae, which assembles into pre-60S ribosomal particles in the nucle(ol)us. Yeast L26 is one of the many ribosomal proteins encoded by two functional genes. We have disrupted both genes; surprisingly, the growth of the resulting rpl26 null mutant is apparently identical to that of the isogenic wild-type strain. The absence of L26 minimally alters 60S ribosomal subunit biogenesis. Polysome analysis revealed the appearance of half-mers. Analysis of pre-rRNA processing indicated that L26 is mainly required to optimize 27S pre-rRNA maturation, without which the release of pre-60S particles from the nucle(ol)us is partially impaired. Ribosomes lacking L26 exhibit differential reactivity to dimethylsulfate in domain I of 25S/5.8S rRNAs but apparently are able to support translation in vivo with wild-type accuracy. The bacterial homologue of yeast L26, L24, is a primary rRNA binding protein required for 50S ribosomal subunit assembly in vitro and in vivo. Our results underscore potential differences between prokaryotic and eukaryotic ribosome assembly. We discuss the reasons why yeast L26 plays such an apparently nonessential role in the cell.

Indexed as

Base SequenceCell NucleolusCrystallizationEvolution, MolecularGreen Fluorescent ProteinsMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationPlasmidsPolyribosomesProtein ConformationReproducibility of ResultsRibosomal ProteinsRibosomesGreen Fluorescent ProteinsRibosomal ProteinsRNARPL26A protein, S cerevisiaeRPL26B protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22688513
PMCPMC3434550
OpenAlexW2112749414

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.