Evidence map›Paper›PMID 25187561›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Molecular mechanics of 30S subunit head rotation.

Srividya Mohan, John Paul Donohue, Harry F Noller

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

70 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. ACS chemical biology · 2026
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  12. 30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  15. Review
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  20. Review

10 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Srividya MohanCenter for Molecular Biology of RNA and Department of Molecular, Cell, and Developmental Biology, University of California at Santa Cruz, Santa Cruz, CA 95064.
John Paul DonohueCenter for Molecular Biology of RNA and Department of Molecular, Cell, and Developmental Biology, University of California at Santa Cruz, Santa Cruz, CA 95064.
Harry F NollerCenter for Molecular Biology of RNA and Department of Molecular, Cell, and Developmental Biology, University of California at Santa Cruz, Santa Cruz, CA 95064 harry@nuvolari.ucsc.edu.
University of California, Santa Cruz · US

Funding

CRYSTAL STRUCTURE OF THE RIBOSOMER01GM059140 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1999 to 2015
$7.2M
RIBOSOME STRUCTURE AND FUNCTIONR01GM017129 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1985 to 2015
$6.9M
NIGMS NIH HHS GM-17929NIGMS NIH HHS GM-59140NIGMS NIH HHS R01 GM017129NIGMS NIH HHS R01 GM059140
6 · The paper itself

Abstract

During ribosomal translocation, a process central to the elongation phase of protein synthesis, movement of mRNA and tRNAs requires large-scale rotation of the head domain of the small (30S) subunit of the ribosome. It has generally been accepted that the head rotates by pivoting around the neck helix (h28) of 16S rRNA, its sole covalent connection to the body domain. Surprisingly, we observe that the calculated axis of rotation does not coincide with the neck. Instead, comparative structure analysis across 55 ribosome structures shows that 30S head movement results from flexing at two hinge points lying within conserved elements of 16S rRNA. Hinge 1, although located within the neck, moves by straightening of the kinked helix h28 at the point of contact with the mRNA. Hinge 2 lies within a three-way helix junction that extends to the body through a second, noncovalent connection; its movement results from flexing between helices h34 and h35 in a plane orthogonal to the movement of hinge 1. Concerted movement at these two hinges accounts for the observed magnitudes of head rotation. Our findings also explain the mode of action of spectinomycin, an antibiotic that blocks translocation by binding to hinge 2.

Indexed as

Models, MolecularRotationBase SequenceEscherichia coliMolecular Sequence DataNucleic Acid ConformationRibosome SubunitsRNA, Ribosomal, 16SSpectinomycinThermus thermophilusRNA, Ribosomal, 16SSpectinomycinRNA dynamicsS5three-way junctiontranslation

Identifiers

PMID25187561
PMCPMC4169957
OpenAlexW2032521665

What OpenQuestion holds

Textmetadata
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.