Evidence map›Paper›PMID 25825718›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Reconstitution of a prokaryotic minus end-tracking system using TubRC centromeric complexes and tubulin-like protein TubZ filaments.

Gero Fink, Jan Löwe

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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
3.1field-weighted citation impact, top 9% 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, 34 citations in OpenAlex.

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  5. Engineering spatiotemporal organization and dynamics in synthetic cells.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021
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  19. Collaborative protein filaments.The EMBO journal · 2015
    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

2 authors at 2 institutions in 1 country.

Gero FinkMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
Jan LöweMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom jyl@mrc-lmb.cam.ac.uk.
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184326Medical Research Council U105184326Wellcome Trust 095514Wellcome Trust 095514/Z/11/Z
6 · The paper itself

Abstract

Segregation of DNA is a fundamental process during cell division. The mechanism of prokaryotic DNA segregation is largely unknown, but several low-copy-number plasmids encode cytomotive filament systems of the actin type and tubulin type important for plasmid inheritance. Of these cytomotive filaments, only actin-like systems are mechanistically well characterized. In contrast, the mechanism by which filaments of tubulin-like TubZ protein mediate DNA motility is unknown. To understand polymer-driven DNA transport, we reconstituted the filaments of TubZ protein (TubZ filaments) from Bacillus thuringiensis pBtoxis plasmid with their centromeric TubRC complexes containing adaptor protein TubR and tubC DNA. TubZ alone assembled into polar filaments, which annealed laterally and treadmilled. Using single-molecule imaging, we show that TubRC complexes were not pushed by filament polymerization; instead, they processively tracked shrinking, depolymerizing minus ends. Additionally, the TubRC complex nucleated TubZ filaments and allowed for treadmilling. Overall, our results indicate a pulling mechanism for DNA transport by the TubZRC system. The discovered minus end-tracking property of the TubRC complex expands the mechanistic diversity of the prokaryotic cytoskeleton.

Indexed as

Bacillus thuringiensisBacterial ProteinsCentromereChromosomes, BacterialCytoskeletal ProteinsCytoskeletonDNA, BacterialMicroscopy, FluorescenceModels, MolecularMutationPlasmidsPolymerizationProtein BindingProtein Structure, SecondaryTubulinBacterial ProteinsCytoskeletal ProteinsDNA, BacterialFtsZ protein, BacteriaTubulincytoskeletonDNA segregationtubulin homologue

Identifiers

PMID25825718
PMCPMC4403160
OpenAlexW2092972430

What OpenQuestion holds

Textmetadata
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.