Evidence map›Paper›PMID 26384427›Full record

ArticleNucleic acids research2015

Conformational toggling controls target site choice for the heteromeric transposase element Tn7.

Qiaojuan Shi, Marco R Straus, Jeremy J Caron, Huasheng Wang, Yu Seon Chung, Alba Guarné, Joseph E Peters

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Bacterial genome engineering using CRISPR RNA-guided transposases.bioRxiv : the preprint server for biology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Recruitment of CRISPR-Cas systems by Tn7-like transposons.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. 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.

Qiaojuan ShiDepartment of Microbiology, Cornell University, Ithaca, NY 14853, USA.
Marco R StrausDepartment of Microbiology, Cornell University, Ithaca, NY 14853, USA.
Jeremy J CaronDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, L8S 4K1, Canada.
Huasheng WangDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, L8S 4K1, Canada.
Yu Seon ChungDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, L8S 4K1, Canada.
Alba GuarnéDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, L8S 4K1, Canada guarnea@mcmaster.ca.
Joseph E PetersDepartment of Microbiology, Cornell University, Ithaca, NY 14853, USA jep48@cornell.edu.

Funding

Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
Tn7 Transpostion into DNA Replication/Repair ComplexesR01GM069508 · NIGMS · CORNELL UNIVERSITY · PI PETERS, JOSEPH E · 2006 to 2010
$1.1M
Canadian Institutes of Health Research MOP-67189NIGMS NIH HHS P41GM103473NIGMS NIH HHS R01 GM069508
6 · The paper itself

Abstract

The bacterial transposon Tn7 facilitates horizontal transfer by directing transposition into actively replicating DNA with the element-encoded protein TnsE. Structural analysis of the C-terminal domain of wild-type TnsE identified a novel protein fold including a central V-shaped loop that toggles between two distinct conformations. The structure of a robust TnsE gain-of-activity variant has this loop locked in a single conformation, suggesting that conformational flexibility regulates TnsE activity. Structure-based analysis of a series of TnsE mutants relates transposition activity to DNA binding stability. Wild-type TnsE appears to naturally form an unstable complex with a target DNA, whereas mutant combinations required for large changes in transposition frequency and targeting stabilized this interaction. Collectively, our work unveils a unique structural proofreading mechanism where toggling between two conformations regulates target commitment by limiting the stability of target DNA engagement until an appropriate insertion site is identified.

Indexed as

DNA Transposable ElementsAlanineBacterial ProteinsDNADNA-Binding ProteinsModels, MolecularMutationProtein FoldingProtein Structure, TertiaryTransposasesAlanineBacterial ProteinsDNADNA-Binding ProteinsDNA Transposable ElementsTransposases

Identifiers

PMID26384427
PMCPMC4678854

What OpenQuestion holds

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LicenceCC BY-NC
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.