Evidence map›Paper›PMID 37316549›Full record

ArticleScientific reports2023

Structural and functional analysis of a plant nucleolar RNA chaperone-like protein.

Rita Fernandes, Anna Ostendorp, Steffen Ostendorp, Judith Mehrmann, Sven Falke, Melissa Ann Graewert, Magdalena Weingartner, Julia Kehr, Stefan Hoth

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Grafting based DNA methylation alteration of snoRNAs in upland cotton (Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
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

9 authors at 4 institutions in 1 country.

Rita FernandesMolecular Plant Physiology, Institute of Plant Science and Microbiology, Department of Biology, Universität Hamburg, Hamburg, Germany.
Anna OstendorpMolecular Plant Genetics, Institute of Plant Science and Microbiology, Department of Biology, Universität Hamburg, Hamburg, Germany.
Steffen OstendorpMolecular Plant Genetics, Institute of Plant Science and Microbiology, Department of Biology, Universität Hamburg, Hamburg, Germany.
Judith MehrmannMolecular Plant Physiology, Institute of Plant Science and Microbiology, Department of Biology, Universität Hamburg, Hamburg, Germany.
Sven FalkeCenter for Free-Electron Laser Science (CFEL), Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, 22607, Hamburg, Germany.
Melissa Ann GraewertEuropean Molecular Biology Laboratory (EMBL) Hamburg Unit, Hamburg, Germany.
Magdalena WeingartnerMolecular Plant Physiology, Institute of Plant Science and Microbiology, Department of Biology, Universität Hamburg, Hamburg, Germany.
Julia KehrMolecular Plant Genetics, Institute of Plant Science and Microbiology, Department of Biology, Universität Hamburg, Hamburg, Germany.
Stefan HothMolecular Plant Physiology, Institute of Plant Science and Microbiology, Department of Biology, Universität Hamburg, Hamburg, Germany. stefan.hoth@uni-hamburg.de.
Universität Hamburg · DEDeutsches Elektronen-Synchrotron DESY · DEEuropean Molecular Biology Laboratory · DEHamburg University of Technology · DE

Funding

European Research Council GA No. 810131
6 · The paper itself

Abstract

Ribosome biogenesis is a key process in all eukaryotic cells that requires hundreds of ribosome biogenesis factors (RBFs), which are essential to build the mature ribosomes consisting of proteins and rRNAs. The processing of the required rRNAs has been studied extensively in yeast and mammals, but in plants much is still unknown. In this study, we focused on a RBF from A. thaliana that we named NUCLEOLAR RNA CHAPERONE-LIKE 1 (NURC1). NURC1 was localized in the nucleolus of plant cell nuclei, and other plant RBF candidates shared the same localization. SEC-SAXS experiments revealed that NURC1 has an elongated and flexible structure. In addition, SEC-MALLS experiments confirmed that NURC1 was present in its monomeric form with a molecular weight of around 28 kDa. RNA binding was assessed by performing microscale thermophoresis with the Arabidopsis internal transcribed spacer 2 (ITS2) of the polycistronic pre-rRNA precursor, which contains the 5.8S, 18S, and 25S rRNA. NURC1 showed binding activity to the ITS2 with a dissociation constant of 228 nM and exhibited RNA chaperone-like activity. Our data suggested that NURC1 may have a function in pre-rRNA processing and thus ribosome biogenesis.

Indexed as

ArabidopsisPlant ProteinsAnimalsMammalsNuclear ProteinsRNARNA PrecursorsScattering, Small AngleX-Ray DiffractionNuclear ProteinsPlant ProteinsRNARNA Precursors

Identifiers

PMID37316549
PMCPMC10267116
OpenAlexW4380627971

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.