Evidence map›Paper›PMID 40884398›Full record

ArticleNucleic acids research2025

Ribosomal protein Rps29/uS14 contributes to 18S rRNA maturation and its abundance regulates osmotic stress response in S. cerevisiae.

Ramin Zadali, Rafal Tomecki, Ulrike Topf

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Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

3 authors.

Ramin ZadaliInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland.
Rafal TomeckiInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland.ORCID 0000-0003-2473-5004
Ulrike TopfInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland.ORCID 0000-0003-2172-2427

Funding

National Science Centre Poland 2017/26/E/NZ1/00724National Science Centre Poland 2019/34/E/NZ1/00367
6 · The paper itself

Abstract

An evolutionarily conserved ribosomal protein Rps29/uS14 participates in the assembly of late pre-40S particles. In yeast Saccharomyces cerevisiae, duplicate genes RPS29A and RPS29B encode two paralogous proteins with 91% sequence identity. Here, we report that loss of either paralog impairs final step of cytoplasmic processing of 20S pre-rRNA, which is a direct precursor of mature 18S ribosomal RNA (rRNA)-a component of small ribosomal subunit. Consistently, we found that late processing factors remain bound to ribosome particles in Rps29-deficient cells. However, pre-40S particles containing 20S pre-rRNA are largely absent from translation-competent 80S ribosomes in Rps29-deficient cells, suggesting that lower levels of Rps29 protein induce quality control steps during maturation of cytoplasmic pre-ribosomal particles. Moreover, we analyzed Rps29 function during cellular stress conditions and found that cells with decreased levels of Rps29 protein adapted more rapidly to osmotic stress, but the effect was independent of the 20S pre-rRNA maturation.

Indexed as

Osmotic PressureRibosomal ProteinsRNA Processing, Post-TranscriptionalRNA, Ribosomal, 18SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGene Expression Regulation, FungalRibosomesRibosome Subunits, Small, EukaryoticRNA PrecursorsRibosomal ProteinsRNA PrecursorsRNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID40884398
PMCPMC12397909

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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.