Evidence map›Paper›PMID 39900920›Full record

ArticleNature communications2025

The assembly factor Reh1 is released from the ribosome during its initial round of translation.

Sharmishtha Musalgaonkar, James N Yelland, Ruta Chitale, Shilpa Rao, Hakan Ozadam, David W Taylor, Can Cenik, Arlen W Johnson

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. 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
–field-weighted citation impact
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.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Sharmishtha Musalgaonkar *Department of Molecular Biosciences, The University of Texas at Austin, Austin, USA.ORCID http://orcid.org/0000-0003-4177-9308
James N Yelland *Interdisciplinary Life Sciences Graduate Program, The University of Texas at Austin, Austin, USA.ORCID http://orcid.org/0000-0002-4816-5117
Ruta ChitaleInterdisciplinary Life Sciences Graduate Program, The University of Texas at Austin, Austin, USA.ORCID http://orcid.org/0009-0009-0220-1352
Shilpa RaoDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, USA.
Hakan OzadamDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, USA.
David W TaylorDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, USA.ORCID http://orcid.org/0000-0002-6198-1194
Can CenikDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, USA. ccenik@austin.utexas.edu.ORCID http://orcid.org/0000-0001-6370-0889
Arlen W JohnsonDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, USA. arlen@utexas.edu.ORCID http://orcid.org/0000-0002-4742-085X

Funding

Eukaryotic Ribosome AssemblyR35GM127127 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Arlen W JOHNSON · 2018 to 2026
$5.6M
Imaging macromolecular machines in gene regulationR35GM138348 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI TAYLOR, DAVID W · 2020 to 2024
$1.9M
Single cell quantification of translation control in early mouse developmentR35GM150667 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Can Cenik · 2023 to 2026
$1.6M
NIGMS NIH HHS R35 GM127127NIGMS NIH HHS R35 GM138348NIGMS NIH HHS R35 GM150667U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM138348
6 · The paper itself

Abstract

Assembly of functional ribosomal subunits and successfully delivering them to the translating pool is a prerequisite for protein synthesis and cell growth. In S. cerevisiae, the ribosome assembly factor Reh1 binds to pre-60S subunits at a late stage during their cytoplasmic maturation. Previous work shows that the C-terminus of Reh1 inserts into the polypeptide exit tunnel of the pre-60S subunit. Here, we show that Reh1-bound nascent 60S subunits associate with 40S subunits to form actively translating ribosomes. Using selective ribosome profiling, we found that Reh1-bound ribosomes populate open reading frames near start codons. Reh1-bound ribosomes are also strongly enriched for initiator tRNA, indicating they are associated with early elongation. Using cryo-electron microscopy to image Reh1-bound 80S ribosomes, we found they contain A site peptidyl tRNA, P site tRNA and eIF5A, indicating that Reh1 does not dissociate from 60S until translation elongation. We propose that Reh1 is displaced by the elongating peptide chain, making it the last assembly factor released from the nascent 60S subunit during its initial round of translation.

Indexed as

Protein BiosynthesisRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCryoelectron MicroscopyEukaryotic Translation Initiation Factor 5AOpen Reading FramesPeptide Chain Elongation, TranslationalPeptide Initiation FactorsProtein BindingRibosome Subunits, Large, EukaryoticRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsRNA, TransferRNA, Transfer, Amino AcylEukaryotic Translation Initiation Factor 5APeptide Initiation FactorsRibosomal ProteinsRNA-Binding ProteinsRNA, TransferRNA, Transfer, Amino AcylSaccharomyces cerevisiae ProteinstRNA, peptidyl-

Identifiers

PMID39900920
PMCPMC11791190

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.