Evidence map›Paper›PMID 24768536›Full record

ArticleMolecular cell2014

Single-molecule imaging of FtsK translocation reveals mechanistic features of protein-protein collisions on DNA.

Ja Yil Lee, Ilya J Finkelstein, Lidia K Arciszewska, David J Sherratt, Eric C Greene

Abstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

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  7. Massively Parallel Profiling of RNA-targeting CRISPR-Cas13d.bioRxiv : the preprint server for biology · 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

5 authors.

Ja Yil LeeDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Ilya J FinkelsteinInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
Lidia K ArciszewskaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
David J SherrattDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Eric C GreeneDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA. Electronic address: ecg2108@columbia.edu.

Funding

Elucidating the Mechanisms of DNA RecombinationR01GM074739 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GREENE, ERIC C · 2006 to 2015
$2.7M
Visualizing the Dynamics of Chromatin and Chromatin Remodeling ProteinsR01GM082848 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GREENE, ERIC C · 2008 to 2016
$2.4M
Single Molecule Studies of DNA Error Recognition by Mismatch Repair EnzymesF32GM080864 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI FINKELSTEIN, ILYA J · 2007 to 2009
$142k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM080864NIGMS NIH HHS F32GM80864NIGMS NIH HHS GM074739NIGMS NIH HHS R01 GM074739NIGMS NIH HHS R01 GM082848Wellcome TrustWellcome Trust WT083469MA
6 · The paper itself

Abstract

In physiological settings, DNA translocases will encounter DNA-bound proteins, which must be dislodged or bypassed to allow continued translocation. FtsK is a bacterial translocase that promotes chromosome dimer resolution and decatenation by activating XerCD-dif recombination. To better understand how translocases act in crowded environments, we used single-molecule imaging to visualize FtsK in real time as it collided with other proteins. We show that FtsK can push, evict, and even bypass DNA-bound proteins. The primary factor dictating the outcome of collisions was the relative affinity of the proteins for their specific binding sites. Importantly, protein-protein interactions between FtsK and XerD help prevent removal of XerCD from DNA by promoting rapid reversal of FtsK. Finally, we demonstrate that RecBCD always overwhelms FtsK when these two motor proteins collide while traveling along the same DNA molecule, indicating that RecBCD is capable of exerting a much greater force than FtsK when translocating along DNA.

Indexed as

Bacteriophage lambdaBinding SitesDNA, BacterialDNA, ViralEscherichia coliEscherichia coli ProteinsMembrane ProteinsPromoter Regions, GeneticProtein Structure, TertiaryProtein TransportDNA, BacterialDNA, ViralEscherichia coli ProteinsFtsK protein, E coliMembrane Proteins

Identifiers

PMID24768536
PMCPMC4048639

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.