Evidence map›Paper›PMID 22538818›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Tubulin homolog TubZ in a phage-encoded partition system.

María A Oliva, Antonio J Martin-Galiano, Yoshihiko Sakaguchi, José M Andreu

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. 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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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

4 authors.

María A OlivaCentro de Investigaciones Biológicas-Consejo Superior de Investigaciones Cientificas, 28040 Madrid, Spain. marian@cib.csic.es
Antonio J Martin-Galiano
Yoshihiko Sakaguchi
José M Andreu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Partition systems are responsible for the process whereby large and essential plasmids are accurately positioned to daughter cells during bacterial division. They are typically made of three components: a centromere-like DNA zone, an adaptor protein, and an assembling protein that is either a Walker-box ATPase (type I) or an actin-like ATPase (type II). A recently described type III segregation system has a tubulin/FtsZ-like protein, called TubZ, for plasmid movement. Here, we present the 2.3 Å structure and dynamic assembly of a TubZ tubulin homolog from a bacteriophage and unravel the Clostridium botulinum phage c-st type III partition system. Using biochemical and biophysical approaches, we prove that a gene upstream from tubZ encodes the partner TubR and localize the centromeric region (tubS), both of which are essential for anchoring phage DNA to the motile TubZ filaments. Finally, we describe a conserved fourth component, TubY, which modulates the TubZ-R-S complex interaction.

Indexed as

Models, MolecularAmino Acid SequenceBacterial ProteinsBacteriophagesBase SequenceBiophysicsCentromereCloning, MolecularClostridium botulinumCluster AnalysisComputational BiologyCrystallizationCytokinesisMolecular Sequence DataMultiprotein ComplexesPhylogenyBacterial Proteinschromosome partition proteins, bacterialMultiprotein ComplexesTubulin

Identifiers

PMID22538818
PMCPMC3356609

What OpenQuestion holds

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Registered trials

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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.