Evidence map›Paper›PMID 36482249›Full record

ArticleNature structural & molecular biology2022

Sequence-specific remodeling of a topologically complex RNP substrate by Spb4.

Victor Emmanuel Cruz, Kamil Sekulski, Nagesh Peddada, Carolin Sailer, Sahana Balasubramanian, Christine S Weirich, Florian Stengel, Jan P Erzberger

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026
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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

8 authors at 5 institutions in 3 countries.

Victor Emmanuel CruzDepartment of Biophysics, UT Southwestern Medical Center - ND10.124B, Dallas, TX, USA.ORCID http://orcid.org/0000-0001-5338-0973
Kamil SekulskiDepartment of Biophysics, UT Southwestern Medical Center - ND10.124B, Dallas, TX, USA.ORCID http://orcid.org/0000-0002-6453-252X
Nagesh PeddadaDepartment of Biophysics, UT Southwestern Medical Center - ND10.124B, Dallas, TX, USA.
Carolin SailerDepartment of Biology, University of Konstanz, Konstanz, Germany.
Sahana BalasubramanianDepartment of Biophysics, UT Southwestern Medical Center - ND10.124B, Dallas, TX, USA.ORCID http://orcid.org/0000-0003-1203-0824
Christine S WeirichDepartment of Biophysics, UT Southwestern Medical Center - ND10.124B, Dallas, TX, USA.ORCID http://orcid.org/0000-0002-9457-881X
Florian StengelDepartment of Biology, University of Konstanz, Konstanz, Germany.ORCID http://orcid.org/0000-0003-1447-4509
Jan P ErzbergerDepartment of Biophysics, UT Southwestern Medical Center - ND10.124B, Dallas, TX, USA. jan.erzberger@utsouthwestern.edu.ORCID http://orcid.org/0000-0002-0266-8835
Southwestern Medical CenterSouthwestern Medical Center · USUniversity of Copenhagen · DKUniversity of Konstanz · DEUniversity of Pittsburgh · US

Funding

Pacific Northwest Center for Cryo-EM - Screening supplementU24GM129547 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI EVANS, JAMES E, GOUAUX, JAMES E · 2018 to 2023
$54.8M
Integrated studies of DEAD-box ATPase function during large ribosomal subunit maturationR01GM135617 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ERZBERGER, JAN PETER · 2020 to 2024
$1.7M
NIGMS NIH HHS R01 GM135617NIGMS NIH HHS U24 GM129547
6 · The paper itself

Abstract

DEAD-box ATPases are ubiquitous enzymes essential in all aspects of RNA biology. However, the limited in vitro catalytic activities described for these enzymes are at odds with their complex cellular roles, most notably in driving large-scale RNA remodeling steps during the assembly of ribonucleoproteins (RNPs). We describe cryo-EM structures of 60S ribosomal biogenesis intermediates that reveal how context-specific RNA unwinding by the DEAD-box ATPase Spb4 results in extensive, sequence-specific remodeling of rRNA secondary structure. Multiple cis and trans interactions stabilize Spb4 in a post-catalytic, high-energy intermediate that drives the organization of the three-way junction at the base of rRNA domain IV. This mechanism explains how limited strand separation by DEAD-box ATPases is leveraged to provide non-equilibrium directionality and ensure efficient and accurate RNP assembly.

Indexed as

DEAD-box RNA HelicasesSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesRibonucleoproteinsRNARNA, RibosomalAdenosine TriphosphatasesDEAD-box RNA HelicasesRibonucleoproteinsRNARNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID36482249
PMCPMC10680166
OpenAlexW4312018782

What OpenQuestion holds

Textmetadata
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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.