Evidence map›Paper›PMID 23209026›Full record

ArticleNucleic acids research2013

Rrp5p, Noc1p and Noc2p form a protein module which is part of early large ribosomal subunit precursors in S. cerevisiae.

Thomas Hierlmeier, Juliane Merl, Martina Sauert, Jorge Perez-Fernandez, Patrick Schultz, Astrid Bruckmann, Stephan Hamperl, Uli Ohmayer, Reinhard Rachel, Anja Jacob and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

49 citing papers in PubMed, 67 citations in OpenAlex.

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  6. The homeostatic regulation of ribosome biogenesis.Seminars in cell & developmental biology · 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

17 authors at 2 institutions in 1 country.

Thomas HierlmeierUniversität Regensburg, Biochemie-Zentrum Regensburg (BZR), Lehrstuhl Biochemie III, 93053 Regensburg, Germany.
Juliane Merl
Martina Sauert
Jorge Perez-Fernandez
Patrick Schultz
Astrid Bruckmann
Stephan Hamperl
Uli Ohmayer
Reinhard Rachel
Anja Jacob
Kristin Hergert
Rainer Deutzmann
Joachim Griesenbeck
Ed Hurt
Philipp Milkereit
Jochen Baßler
Herbert Tschochner
Heidelberg University · DEUniversity of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic ribosome biogenesis requires more than 150 auxiliary proteins, which transiently interact with pre-ribosomal particles. Previous studies suggest that several of these biogenesis factors function together as modules. Using a heterologous expression system, we show that the large ribosomal subunit (LSU) biogenesis factor Noc1p of Saccharomyces cerevisiae can simultaneously interact with the LSU biogenesis factor Noc2p and Rrp5p, a factor required for biogenesis of the large and the small ribosomal subunit. Proteome analysis of RNA polymerase-I-associated chromatin and chromatin immunopurification experiments indicated that all members of this protein module and a specific set of LSU biogenesis factors are co-transcriptionally recruited to nascent ribosomal RNA (rRNA) precursors in yeast cells. Further ex vivo analyses showed that all module members predominantly interact with early pre-LSU particles after the initial pre-rRNA processing events have occurred. In yeast strains depleted of Noc1p, Noc2p or Rrp5p, levels of the major LSU pre-rRNAs decreased and the respective other module members were associated with accumulating aberrant rRNA fragments. Therefore, we conclude that the module exhibits several binding interfaces with pre-ribosomes. Taken together, our results suggest a co- and post-transcriptional role of the yeast Rrp5p-Noc1p-Noc2p module in the structural organization of early LSU precursors protecting them from non-productive RNase activity.

Indexed as

AnimalsBinding SitesCarrier ProteinsCell LineDNA-Binding ProteinsNuclear ProteinsRecombinant ProteinsRibosome Subunits, Large, EukaryoticRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTranscription, GeneticCarrier ProteinsDNA-Binding ProteinsMAK21 protein, S cerevisiaeNOC2 protein, S cerevisiaeNuclear ProteinsRecombinant ProteinsRNA-Binding ProteinsRRP5 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID23209026
PMCPMC3553968
OpenAlexW2128583043

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.