Evidence map›Paper›PMID 26237581›Full record

ArticleRNA biology2015

hUTP24 is essential for processing of the human rRNA precursor at site A1, but not at site A0.

Rafal Tomecki, Anna Labno, Karolina Drazkowska, Dominik Cysewski, Andrzej Dziembowski

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

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  9. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 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

5 authors at 2 institutions in 1 country.

Rafal Tomeckia Institute of Biochemistry and Biophysics; Polish Academy of Sciences ; Warsaw , Poland.
Anna Labnoa Institute of Biochemistry and Biophysics; Polish Academy of Sciences ; Warsaw , Poland.
Karolina Drazkowskaa Institute of Biochemistry and Biophysics; Polish Academy of Sciences ; Warsaw , Poland.
Dominik Cysewskia Institute of Biochemistry and Biophysics; Polish Academy of Sciences ; Warsaw , Poland.
Andrzej Dziembowskia Institute of Biochemistry and Biophysics; Polish Academy of Sciences ; Warsaw , Poland.
University of Warsaw · PLInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Production of ribosomes relies on more than 200 accessory factors to ensure the proper sequence of steps and faultless assembly of ribonucleoprotein machinery. Among trans-acting factors are numerous enzymes, including ribonucleases responsible for processing the large rRNA precursor synthesized by RNA polymerase I that encompasses sequences corresponding to mature 18S, 5.8S, and 25/28S rRNA. In humans, the identity of most enzymes responsible for individual processing steps, including endoribonucleases that cleave pre-rRNA at specific sites within regions flanking and separating mature rRNA, remains largely unknown. Here, we investigated the role of hUTP24 in rRNA maturation in human cells. hUTP24 is a human homolog of the Saccharomyces cerevisiae putative PIN domain-containing endoribonuclease Utp24 (yUtp24), which was suggested to participate in the U3 snoRNA-dependent processing of yeast pre-rRNA at sites A0, A1, and A2. We demonstrate that hUTP24 interacts to some extent with proteins homologous to the components of the yeast small subunit (SSU) processome. Moreover, mutation in the putative catalytic site of hUTP24 results in slowed growth of cells and reduced metabolic activity. These effects are associated with a defect in biogenesis of the 40S ribosomal subunit, which results from decreased amounts of 18S rRNA as a consequence of inaccurate pre-rRNA processing at the 5'-end of the 18S rRNA segment (site A1). Interestingly, and in contrast to yeast, site A0 located upstream of A1 is efficiently processed upon UTP24 dysfunction. Finally, hUTP24 inactivation leads to aberrant processing of 18S rRNA 2 nucleotides downstream of the normal A1 cleavage site.

Indexed as

Genes, rRNARNA Processing, Post-TranscriptionalAmino Acid SequenceCarrier ProteinsCatalytic DomainCell ProliferationDEAD-box RNA HelicasesGene ExpressionGene Knockdown TechniquesGenetic Complementation TestHeLa CellsHumansMolecular Sequence DataMutationNuclear ProteinsProtein BindingCarrier ProteinsDEAD-box RNA HelicasesFCF1 protein, humanFcf1 protein, S cerevisiaeNuclear ProteinsRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarRNA, U3 small nucleolarSaccharomyces cerevisiae ProteinsEndoribonucleaserRNArRNA processingSSU processomeU3 snoRNAUTP24

Identifiers

PMID26237581
PMCPMC4615547
OpenAlexW1923293781

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.