Evidence map›Paper›PMID 23599494›Full record

ArticleScience (New York, N.Y.)2013

The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA.

Friedrich W Schwarz, Júlia Tóth, Kara van Aelst, Guanshen Cui, Sylvia Clausing, Mark D Szczelkun, Ralf Seidel

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.8field-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

47 citing papers in PubMed, 84 citations in OpenAlex.

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  6. Hachiman is a genome integrity sensor.bioRxiv : the preprint server for biology · 2024
    Article
  7. Changing protein-DNA interactions promote ORC binding-site exchange during replication origin licensing.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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 at 1 institution in 1 country.

Friedrich W SchwarzDNA motors group, Biotechnology Center, Technische Universität Dresden, 01062 Dresden, Germany.
Júlia Tóth
Kara van Aelst
Guanshen Cui
Sylvia Clausing
Mark D Szczelkun
Ralf Seidel
University of Bristol · GB

Funding

European Research Council 261224Wellcome Trust 084086
6 · The paper itself

Abstract

Helicases are ubiquitous adenosine triphosphatases (ATPases) with widespread roles in genome metabolism. Here, we report a previously undescribed functionality for ATPases with helicase-like domains; namely, that ATP hydrolysis can trigger ATP-independent long-range protein diffusion on DNA in one dimension (1D). Specifically, using single-molecule fluorescence microscopy we show that the Type III restriction enzyme EcoP15I uses its ATPase to switch into a distinct structural state that diffuses on DNA over long distances and long times. The switching occurs only upon binding to the target site and requires hydrolysis of ~30 ATPs. We define the mechanism for these enzymes and show how ATPase activity is involved in DNA target site verification and 1D signaling, roles that are common in DNA metabolism: for example, in nucleotide excision and mismatch repair.

Indexed as

DNA CleavageAdenosine TriphosphateDeoxyribonucleases, Type III Site-SpecificDNADNA HelicasesHydrolysisMicroscopy, FluorescenceNucleic Acid ConformationProtein Structure, TertiaryAdenosine TriphosphateDeoxyribonucleases, Type III Site-SpecificDNADNA Helicasesendodeoxyribonuclease EcoP15I

Identifiers

PMID23599494
PMCPMC3646237
OpenAlexW2040546014

What OpenQuestion holds

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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.