Evidence map›Paper›PMID 24481252›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Accessory factors promote AlfA-dependent plasmid segregation by regulating filament nucleation, disassembly, and bundling.

Jessica K Polka, Justin M Kollman, R Dyche Mullins

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  12. Cryo-EM reconstruction of AlfA fromProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Review
  14. Review
  15. Article
  16. Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Review
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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

3 authors at 2 institutions in 2 countries.

Jessica K PolkaDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158.
Justin M Kollman
R Dyche Mullins
University of California, San Francisco · USMcGill University · CA

Funding

MECHANISMS OF ARP2/3 ACTIVATION AND FUNCTIONR01GM061010 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2000 to 2015
$3.8M
Regulation and Function of a Bacterial CytoskeletonR01GM079556 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2006 to 2015
$2.1M
Assembly dynamics and cellular function of Actin-like proteins in bacteriaR01GM095263 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2010 to 2013
$1.4M
Mechanism and function of a novel actin nucleatorR01GM075287 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2006 to 2009
$1.0M
NIGMS NIH HHS R01 GM061010NIGMS NIH HHS R01 GM075287NIGMS NIH HHS R01 GM079556NIGMS NIH HHS R01GM079556NIGMS NIH HHS R01 GM095263NIGMS NIH HHS R01GM095263
6 · The paper itself

Abstract

In bacteria, some plasmids are partitioned to daughter cells by assembly of actin-like proteins (ALPs). The best understood ALP, ParM, has a core set of biochemical properties that contributes to its function, including dynamic instability, spontaneous nucleation, and bidirectional elongation. AlfA, an ALP that pushes plasmids apart in Bacillus, relies on a different set of underlying properties to segregate DNA. AlfA elongates unidirectionally and is not dynamically unstable; its assembly and disassembly are regulated by a cofactor, AlfB. Free AlfB breaks up AlfA bundles and promotes filament turnover. However, when AlfB is bound to the centromeric DNA sequence, parN, it forms a segrosome complex that nucleates and stabilizes AlfA filaments. When reconstituted in vitro, this system creates polarized, motile comet tails that associate by antiparallel filament bundling to form bipolar, DNA-segregating spindles.

Indexed as

PlasmidsBacillus subtilisBacterial ProteinsCentromereDNA, BacterialOperonProtein ConformationBacterial ProteinsDNA, BacterialBacillus subtilisbacterial cytoskeletonDNA segregationreconstitution

Identifiers

PMID24481252
PMCPMC3926056
OpenAlexW2108017448

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.