Evidence map›Paper›PMID 25294832›Full record

ArticleNucleic acids research2014

Mechanical force antagonizes the inhibitory effects of RecX on RecA filament formation in Mycobacterium tuberculosis.

Shimin Le, Hu Chen, Xinghua Zhang, Jin Chen, K Neelakanteshwar Patil, Kalappa Muniyappa, Jie Yan

Abstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Single-molecule force spectroscopy reveals intra- and intermolecular interactions ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. Article
  5. Targeting evolution of antibiotic resistance by SOS response inhibition.Computational and structural biotechnology journal · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

7 authors.

Shimin LeMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore Department of Physics, National University of Singapore, Singapore 117542, Singapore.
Hu ChenMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore Department of Physics, Xiamen University, Xiamen 361005, China.
Xinghua ZhangBioSystems and Micromechanics (BioSyM) IRG, Singapore-MIT Alliance for Research and Technology, National University of Singapore, Singapore 138602, Singapore.
Jin ChenMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
K Neelakanteshwar PatilDepartment of Biochemistry, Indian Institute of Science, Bangalore 560012, India.
Kalappa MuniyappaDepartment of Biochemistry, Indian Institute of Science, Bangalore 560012, India phyyj@nus.edu.sg.
Jie YanMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore Department of Physics, National University of Singapore, Singapore 117542, Singapore Centre for Bioimaging Sciences, National University of Singapore, Singapore 117557, Singapore phyyj@nus.edu.sg.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Efficient bacterial recombinational DNA repair involves rapid cycles of RecA filament assembly and disassembly. The RecX protein plays a crucial inhibitory role in RecA filament formation and stability. As the broken ends of DNA are tethered during homologous search, RecA filaments assembled at the ends are likely subject to force. In this work, we investigated the interplay between RecX and force on RecA filament formation and stability. Using magnetic tweezers, at single molecular level, we found that Mycobacterium tuberculosis (Mt) RecX could catalyze stepwise de-polymerization of preformed MtRecA filament in the presence of ATP hydrolysis at low forces (<7 pN). However, applying larger forces antagonized the inhibitory effects of MtRecX, and a partially de-polymerized MtRecA filament could re-polymerize in the presence of MtRecX, which cannot be explained by previous models. Theoretical analysis of force-dependent conformational free energies of naked ssDNA and RecA nucleoprotein filament suggests that mechanical force stabilizes RecA filament, which provides a possible mechanism for the observation. As the antagonizing effect of force on the inhibitory function of RecX takes place in a physiological range; these findings broadly suggest a potential mechanosensitive regulation during homologous recombination.

Indexed as

Adenosine TriphosphateBacterial ProteinsBiomechanical PhenomenaDNA, Single-StrandedMycobacterium tuberculosisPolymerizationRec A RecombinasesAdenosine TriphosphateBacterial ProteinsDNA, Single-StrandedRec A Recombinases

Identifiers

PMID25294832
PMCPMC4231760

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Registered trials

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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.