Evidence map›Paper›PMID 22885300›Full record

ArticleNucleic acids research2012

The processing of repetitive extragenic palindromes: the structure of a repetitive extragenic palindrome bound to its associated nuclease.

Simon A J Messing, Bao Ton-Hoang, Alison B Hickman, Andrew J McCubbin, Graham F Peaslee, Rodolfo Ghirlando, Michael Chandler, Fred Dyda

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structural variability of CG-rich DNA 18-mers accommodating double T-T mismatches.Acta crystallographica. Section D, Structural biology · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Mechanisms of DNA Transposition.Microbiology spectrum · 2015
    Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
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 2 institutions in 1 country.

Simon A J MessingLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Bao Ton-Hoang
Alison B Hickman
Andrew J McCubbin
Graham F Peaslee
Rodolfo Ghirlando
Michael Chandler
Fred Dyda
National Institutes of Health · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Structure and function of novel prokaryotic DNA transposasesZIADK036154 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI DYDA, FREDERICK · 2009 to 2023
$7.7M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Intramural NIH HHS
6 · The paper itself

Abstract

Extragenic sequences in genomes, such as microRNA and CRISPR, are vital players in the cell. Repetitive extragenic palindromic sequences (REPs) are a class of extragenic sequences, which form nucleotide stem-loop structures. REPs are found in many bacterial species at a high copy number and are important in regulation of certain bacterial functions, such as Integration Host Factor recruitment and mRNA turnover. Although a new clade of putative transposases (RAYTs or TnpA(REP)) is often associated with an increase in these repeats, it is not clear how these proteins might have directed amplification of REPs. We report here the structure to 2.6 Å of TnpA(REP) from Escherichia coli MG1655 bound to a REP. Sequence analysis showed that TnpA(REP) is highly related to the IS200/IS605 family, but in contrast to IS200/IS605 transposases, TnpA(REP) is a monomer, is auto-inhibited and is active only in manganese. These features suggest that, relative to IS200/IS605 transposases, it has evolved a different mechanism for the movement of discrete segments of DNA and has been severely down-regulated, perhaps to prevent REPs from sweeping through genomes.

Indexed as

Inverted Repeat SequencesAmino Acid SequenceCatalytic DomainDeoxyribonucleasesDNA, BacterialDNA CleavageEscherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataSequence AlignmentTransposasesDeoxyribonucleasesDNA, BacterialEscherichia coli ProteinsTnpA(rep) protein, E coliTransposases

Identifiers

PMID22885300
PMCPMC3479197
OpenAlexW2133671956

What OpenQuestion holds

Textmetadata
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.