Evidence map›Paper›PMID 31115337›Full record

ArticleeLife2019

Mechanism of completion of peptidyltransferase centre assembly in eukaryotes.

Vasileios Kargas, Pablo Castro-Hartmann, Norberto Escudero-Urquijo, Kyle Dent, Christine Hilcenko, Carolin Sailer, Gertrude Zisser, Maria J Marques-Carvalho, Simone Pellegrino, Leszek Wawiórka and 8 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  3. Structure of a Gcn2 dimer in complex with the large 60S ribosomal subunit.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

18 authors at 6 institutions in 4 countries.

Vasileios Kargas *Cambridge Institute for Medical Research, Cambridge, United Kingdom.ORCID 0000-0001-8588-7285
Pablo Castro-Hartmann *Cambridge Institute for Medical Research, Cambridge, United Kingdom.
Norberto Escudero-UrquijoCambridge Institute for Medical Research, Cambridge, United Kingdom.ORCID 0000-0002-8201-5884
Kyle DentCambridge Institute for Medical Research, Cambridge, United Kingdom.
Christine HilcenkoCambridge Institute for Medical Research, Cambridge, United Kingdom.
Carolin SailerDepartment of Biology, University of Konstanz, Konstanz, Germany.ORCID 0000-0001-7735-6070
Gertrude ZisserInstitute of Molecular Biosciences, University of Graz, Graz, Austria.
Maria J Marques-CarvalhoCambridge Institute for Medical Research, Cambridge, United Kingdom.
Simone PellegrinoCambridge Institute for Medical Research, Cambridge, United Kingdom.
Leszek WawiórkaCambridge Institute for Medical Research, Cambridge, United Kingdom.
Stefan Mv FreundMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Jane L WagstaffMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Antonina AndreevaMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Alexandre FailleCambridge Institute for Medical Research, Cambridge, United Kingdom.
Edwin ChenFaculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0003-0742-9734
Florian StengelDepartment of Biology, University of Konstanz, Konstanz, Germany.ORCID 0000-0003-1447-4509
Helmut BerglerInstitute of Molecular Biosciences, University of Graz, Graz, Austria.ORCID 0000-0002-7724-309X
Alan John WarrenCambridge Institute for Medical Research, Cambridge, United Kingdom.ORCID 0000-0001-9277-4553
Wellcome/MRC Cambridge Stem Cell Institute · GBMRC Laboratory of Molecular Biology · GBUniversity of Graz · ATUniversity of Konstanz · DEMaria Curie-Skłodowska University · PLUniversity of Leeds · GB

Funding

Austrian Science Fund FWF P 26136Austrian Science Fund FWF P 29451Blood Cancer UK 12048Medical Research Council MC_PC_12009Medical Research Council MC_U105161083Medical Research Council MC_U105184326Medical Research Council MC_UP_1201/14Medical Research Council MR/L003368/1
6 · The paper itself

Abstract

During their final maturation in the cytoplasm, pre-60S ribosomal particles are converted to translation-competent large ribosomal subunits. Here, we present the mechanism of peptidyltransferase centre (PTC) completion that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3. Single-particle cryo-EM reveals that eL40 recruitment stabilises helix 89 to form the uL16 binding site. The loading of uL16 unhooks helix 38 from Nmd3 to adopt its mature conformation. In turn, partial retraction of the L1 stalk is coupled to a conformational switch in Nmd3 that allows the uL16 P-site loop to fully accommodate into the PTC where it competes with Nmd3 for an overlapping binding site (base A2971). Our data reveal how the central functional site of the ribosome is sculpted and suggest how the formation of translation-competent 60S subunits is disrupted in leukaemia-associated ribosomopathies.

Indexed as

Cryoelectron MicroscopyPeptidyl TransferasesRibosomal ProteinsRibosome Subunits, Large, EukaryoticRNA, RibosomalSaccharomyces cerevisiaePeptidyl TransferasesRibosomal ProteinsRNA, Ribosomalcryo-EMleukaemiamolecular biophysicsribosomeribosomopathySBDSS. cerevisiaeShwachman-Diamond syndromestructural biology

Identifiers

PMID31115337
PMCPMC6579518
OpenAlexW2946528398

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.