Evidence map›Paper›PMID 24207057›Full record

ArticleMolecular cell2013

In vivo X-ray footprinting of pre-30S ribosomes reveals chaperone-dependent remodeling of late assembly intermediates.

Sarah F Clatterbuck Soper, Romel P Dator, Patrick A Limbach, Sarah A Woodson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 104 citations in OpenAlex.

  1. Methyltransferase RsmB chaperonesScience advances · 2026
    Article
  2. Review
  3. Article
  4. Article
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  6. Mechanistic insights intobioRxiv : the preprint server for biology · 2026
    Article
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14 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Sarah F Clatterbuck SoperCell, Molecular, and Developmental Biology and Biophysics Program, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218-2685, USA.
Romel P Dator
Patrick A Limbach
Sarah A Woodson
Johns Hopkins University · USUniversity of Cincinnati · US

Funding

TIME RESOLVED HYDROXYL RADICAL FOOTPRINTING OF RNAR01GM060819 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOODSON, SARAH A. · 1999 to 2019
$6.1M
UPLC for Enhanced Mass Spectrometry of Modified RNAsR01GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 1999 to 2025
$5.1M
Assessment of Tissue Response to StressR01EB000998 · NIBIB · UNIVERSITY OF WASHINGTON · PI SANDERS, JOAN E · 2003 to 2006
$1.1M
Acquisition of an LC Mass Spectrometer for Nucleic Acids ResearchS10RR027671 · NCRR · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 2010 to 2010
$500k
Mass Spectrometry of Ribosomal RNA:Protein InteractionsR56GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 2009 to 2009
$330k
NCRR NIH HHS RR027671NCRR NIH HHS S10 RR027671NIBIB NIH HHS P30-EB-00998NIBIB NIH HHS R01 EB000998NIGMS NIH HHS GM58843NIGMS NIH HHS GM60819NIGMS NIH HHS R01 GM058843NIGMS NIH HHS R01 GM060819NIGMS NIH HHS R56 GM058843
6 · The paper itself

Abstract

Assembly of 30S ribosomal subunits from their protein and RNA components requires extensive refolding of the 16S rRNA and is assisted by 10-20 assembly factors in bacteria. We probed the structures of 30S assembly intermediates in E. coli cells, using a synchrotron X-ray beam to generate hydroxyl radical in the cytoplasm. Widespread differences between mature and pre-30S complexes in the absence of assembly factors RbfA and RimM revealed global reorganization of RNA-protein interactions prior to maturation of the 16S rRNA and showed how RimM reduces misfolding of the 16S 3' domain during transcription in vivo. Quantitative (14)N/(15)N mass spectrometry of affinity-purified pre-30S complexes confirmed the absence of tertiary assembly proteins and showed that N-terminal acetylation of proteins S18 and S5 correlates with correct folding of the platform and central pseudoknot. Our results indicate that cellular factors delay specific RNA folding steps to ensure the quality of assembly.

Indexed as

AcetylationEscherichia coliEscherichia coli ProteinsGene DeletionInverted Repeat SequencesModels, MolecularMolecular ChaperonesNucleic Acid ConformationProtein MultimerizationProtein Processing, Post-TranslationalRibosomal ProteinsRibosome Subunits, Small, BacterialRNA CleavageRNA FoldingRNA, Ribosomal, 16STranscription, GeneticEscherichia coli ProteinsMolecular ChaperonesRbfA protein, E coliRibosomal ProteinsRimM protein, E coliRNA, Ribosomal, 16S

Identifiers

PMID24207057
PMCPMC3840108
OpenAlexW2006438017

What OpenQuestion holds

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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.