Evidence map›Paper›PMID 31471187›Full record

ArticleMolecular cell2019

Co-temporal Force and Fluorescence Measurements Reveal a Ribosomal Gear Shift Mechanism of Translation Regulation by Structured mRNAs.

Varsha P Desai, Filipp Frank, Antony Lee, Maurizio Righini, Laura Lancaster, Harry F Noller, Ignacio Tinoco, Carlos Bustamante

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 63 citations in OpenAlex.

  1. RNAViruses · 2026
    Review
  2. Article
  3. Article
  4. Ribosome-induced mRNA pseudoknot interactions visualized by DMS MaP-Seq.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Assignment of structural transitions during mechanical unwrapping of nucleosomes and their disassembly products.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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 3 institutions in 1 country.

Varsha P DesaiDepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA; Jason L. Choy Laboratory of Single-Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94720, USA.
Filipp FrankJason L. Choy Laboratory of Single-Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94720, USA.
Antony LeeJason L. Choy Laboratory of Single-Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Physics, University of California, Berkeley, Berkeley, CA 94720, USA.
Maurizio RighiniDepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA; Jason L. Choy Laboratory of Single-Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences, QB3, University of California, Berkeley, Berkeley, CA 94720, USA.
Laura LancasterDepartment of Molecular, Cell, and Developmental Biology and Center for Molecular Biology of RNA, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.
Harry F NollerDepartment of Molecular, Cell, and Developmental Biology and Center for Molecular Biology of RNA, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.
Ignacio TinocoDepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.
Carlos BustamanteDepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA; Jason L. Choy Laboratory of Single-Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Physics, University of California, Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences, QB3, University of California, Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA; Kavli Energy Nanoscience Institute, University of California, Berkeley, Berkeley, CA 94720, USA. Electronic address: carlosb@berkeley.edu.
University of California, Berkeley · USUniversity of California, Santa Cruz · USQB3 · US

Funding

Ribosome Structure and FunctionR35GM118156 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 2016 to 2025
$7.8M
THE PHYSICAL CHEMISTRY OF NUCLEIC ACIDSR01GM032543 · NIGMS · UNIVERSITY OF OREGON · PI CARLOS Jose BUSTAMANTE · 1985 to 2026
$6.4M
Mechanisms of Viral DNA PackagingR01GM071552 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BUSTAMANTE, CARLOS JOSE · 2004 to 2015
$4.7M
PHYSICAL CHEMISTRY OF NUCLEIC ACIDSR37GM032543 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BUSTAMANTE, CARLOS JOSE · 1999 to 2008
$2.4M
NIGMS NIH HHS R01 GM032543NIGMS NIH HHS R01 GM071552NIGMS NIH HHS R35 GM118156NIGMS NIH HHS R37 GM032543
6 · The paper itself

Abstract

The movement of ribosomes on mRNA is often interrupted by secondary structures that present mechanical barriers and play a central role in translation regulation. We investigate how ribosomes couple their internal conformational changes with the activity of translocation factor EF-G to unwind mRNA secondary structures using high-resolution optical tweezers with single-molecule fluorescence capability. We find that hairpin opening occurs during EF-G-catalyzed translocation and is driven by the forward rotation of the small subunit head. Modulating the magnitude of the hairpin barrier by force shows that ribosomes respond to strong barriers by shifting their operation to an alternative 7-fold-slower kinetic pathway prior to translocation. Shifting into a slow gear results from an allosteric switch in the ribosome that may allow it to exploit thermal fluctuations to overcome mechanical barriers. Finally, we observe that ribosomes occasionally open the hairpin in two successive sub-codon steps, revealing a previously unobserved translocation intermediate.

Indexed as

Nucleic Acid ConformationOptical TweezersEscherichia coliFluorescenceRibosomesRNA, BacterialRNA, MessengerRNA, BacterialRNA, Messengerallosteric switchmRNA secondary structuresoptical tweezersribosomal gear shiftribosomesingle-molecule fluorescencetranslation regulationtranslocation mechanism

Identifiers

PMID31471187
PMCPMC6779417
OpenAlexW2970308379

What OpenQuestion holds

Textmetadata
LicenceTDM
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.