Evidence map›Paper›PMID 24880688›Full record

ArticleNucleic acids research2014

A highly processive topoisomerase I: studies at the single-molecule level.

Marcin Jan Szafran, Terence Strick, Agnieszka Strzałka, Jolanta Zakrzewska-Czerwińska, Dagmara Jakimowicz

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Mechanistic basis for relaxation of DNA supercoils by human topoisomerase IIIα-RMI1-RMI2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Mechanism of Type IA Topoisomerases.Molecules (Basel, Switzerland) · 2020
    Review
  8. Direct observation of helicase-topoisomerase coupling within reverse gyrase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Review
  10. Article
  11. Transcriptional Response ofFrontiers in microbiology · 2019
    Article
  12. Frontiers in cellular and infection microbiology · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

5 authors.

Marcin Jan SzafranFaculty of Biotechnology, University of Wrocław, Joliot-Curie 14A, 50-383 Wrocław, Poland marcin.szafran@uni.wroc.pl.
Terence StrickInstitut Jacques Monod, CNRS UMR 7592, University Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France strick.terence@ijm.univ-paris-diderot.fr.
Agnieszka StrzałkaFaculty of Biotechnology, University of Wrocław, Joliot-Curie 14A, 50-383 Wrocław, Poland.
Jolanta Zakrzewska-CzerwińskaFaculty of Biotechnology, University of Wrocław, Joliot-Curie 14A, 50-383 Wrocław, Poland Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, Wrocław, 53-114, Poland.
Dagmara JakimowiczFaculty of Biotechnology, University of Wrocław, Joliot-Curie 14A, 50-383 Wrocław, Poland Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, Wrocław, 53-114, Poland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amongst enzymes which relieve torsional strain and maintain chromosome supercoiling, type IA topoisomerases share a strand-passage mechanism that involves transient nicking and re-joining of a single deoxyribonucleic acid (DNA) strand. In contrast to many bacterial species that possess two type IA topoisomerases (TopA and TopB), Actinobacteria possess only TopA, and unlike its homologues this topoisomerase has a unique C-terminal domain that lacks the Zn-finger motifs characteristic of type IA enzymes. To better understand how this unique C-terminal domain affects the enzyme's activity, we have examined DNA relaxation by actinobacterial TopA from Streptomyces coelicolor (ScTopA) using real-time single-molecule experiments. These studies reveal extremely high processivity of ScTopA not described previously for any other topoisomerase of type I. Moreover, we also demonstrate that enzyme processivity varies in a torque-dependent manner. Based on the analysis of the C-terminally truncated ScTopA mutants, we propose that high processivity of the enzyme is associated with the presence of a stretch of positively charged amino acids in its C-terminal region.

Indexed as

Bacterial ProteinsDNADNA, SuperhelicalDNA Topoisomerases, Type IStreptomyces coelicolorTorqueBacterial ProteinsDNADNA, SuperhelicalDNA Topoisomerases, Type I

Identifiers

PMID24880688
PMCPMC4081095

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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.