Evidence map›Paper›PMID 28575120›Full record

ArticlePloS one2017

Structural basis for 5'-ETS recognition by Utp4 at the early stages of ribosome biogenesis.

Fabiola R Calviño, Markus Kornprobst, Géza Schermann, Fabienne Birkle, Klemens Wild, Tamas Fischer, Ed Hurt, Yasar Luqman Ahmed, Irmgard Sinning

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  4. Article
  5. Review
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 1 institution in 1 country.

Fabiola R CalviñoHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Markus KornprobstHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Géza SchermannHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Fabienne BirkleHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Klemens WildHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Tamas FischerHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Ed HurtHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Yasar Luqman AhmedHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
Irmgard SinningHeidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-9127-4477
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic ribosome biogenesis begins with the co-transcriptional assembly of the 90S pre-ribosome. The 'U three protein' (UTP) complexes and snoRNP particles arrange around the nascent pre-ribosomal RNA chaperoning its folding and further maturation. The earliest event in this hierarchical process is the binding of the UTP-A complex to the 5'-end of the pre-ribosomal RNA (5'-ETS). This oligomeric complex predominantly consists of β-propeller and α-solenoidal proteins. Here we present the structure of the Utp4 subunit from the thermophilic fungus Chaetomium thermophilum at 2.15 Å resolution and analyze its function by UV RNA-crosslinking (CRAC) and in context of a recent cryo-EM structure of the 90S pre-ribosome. Utp4 consists of two orthogonal and highly basic β-propellers that perfectly fit the EM-data. The Utp4 structure highlights an unusual Velcro-closure of its C-terminal β-propeller as relevant for protein integrity and potentially Utp8 recognition in the context of the pre-ribosome. We provide a first model of the 5'-ETS RNA from the internally hidden 5'-end up to the region that hybridizes to the 3'-hinge sequence of U3 snoRNA and validate a specific Utp4/5'-ETS interaction by CRAC analysis.

Indexed as

Organelle BiogenesisChaetomiumCryoelectron MicroscopyFungal ProteinsModels, MolecularNucleic Acid ConformationProtein BindingProtein ConformationProtein SubunitsRibonucleoproteinsRibosomesRNA PrecursorsTranscription, GeneticFungal ProteinsProtein SubunitsRibonucleoproteinsRNA Precursors

Identifiers

PMID28575120
PMCPMC5456268
OpenAlexW2620746405

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.