Evidence map›Paper›PMID 27016742›Full record

ArticleNucleic acids research2016

Force regulated dynamics of RPA on a DNA fork.

Felix E Kemmerich, Peter Daldrop, Cosimo Pinto, Maryna Levikova, Petr Cejka, Ralf Seidel

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-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

24 citing papers in PubMed, 36 citations in OpenAlex.

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  9. "Helicase" Activity promoted through dynamic interactions between a ssDNA translocase and a diffusing SSB protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors at 3 institutions in 2 countries.

Felix E KemmerichInstitute of Experimental Physics I, Universität Leipzig, Linnéstr. 5, 04103 Leipzig, Germany Institute for Molecular Cell Biology, University of Münster, Schlossplatz 5, D-48149 Münster, Germany.
Peter DaldropInstitute for Molecular Cell Biology, University of Münster, Schlossplatz 5, D-48149 Münster, Germany.
Cosimo PintoInstitute of Molecular Cancer Research, University of Zurich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
Maryna LevikovaInstitute of Molecular Cancer Research, University of Zurich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
Petr CejkaInstitute of Molecular Cancer Research, University of Zurich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
Ralf SeidelInstitute of Experimental Physics I, Universität Leipzig, Linnéstr. 5, 04103 Leipzig, Germany Institute for Molecular Cell Biology, University of Münster, Schlossplatz 5, D-48149 Münster, Germany ralf.seidel@physik.uni-leipzig.de.
University of Zurich · CHUniversity of Münster · DELeipzig University · DE

Funding

European Research Council 261224
6 · The paper itself

Abstract

Replication protein A (RPA) is a single-stranded DNA binding protein, involved in most aspects of eukaryotic DNA metabolism. Here, we study the behavior of RPA on a DNA substrate that mimics a replication fork. Using magnetic tweezers we show that both yeast and human RPA can open forked DNA when sufficient external tension is applied. In contrast, at low force, RPA becomes rapidly displaced by the rehybridization of the DNA fork. This process appears to be governed by the binding or the release of an RPA microdomain (toehold) of only few base-pairs length. This gives rise to an extremely rapid exchange dynamics of RPA at the fork. Fork rezipping rates reach up to hundreds of base-pairs per second, being orders of magnitude faster than RPA dissociation from ssDNA alone. Additionally, we show that RPA undergoes diffusive motion on ssDNA, such that it can be pushed over long distances by a rezipping fork. Generally the behavior of both human and yeast RPA homologs is very similar. However, in contrast to yeast RPA, the dissociation of human RPA from ssDNA is greatly reduced at low Mg(2+) concentrations, such that human RPA can melt DNA in absence of force.

Indexed as

DNA ReplicationMechanotransduction, CellularBiomechanical PhenomenaCloning, MolecularDNA, Single-StrandedEscherichia coliGene ExpressionHumansInverted Repeat SequencesMagnesiumMagnetic FieldsNucleic Acid DenaturationOptical TweezersRecombinant ProteinsReplication Protein ASaccharomyces cerevisiaeDNA, Single-StrandedMagnesiumRecombinant ProteinsReplication Protein ARFA1 protein, S cerevisiaeRPA1 protein, humanSaccharomyces cerevisiae Proteins

Identifiers

PMID27016742
PMCPMC4937307
OpenAlexW2316204282

What OpenQuestion holds

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LicenceCC BY
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.