Evidence map›Paper›PMID 16484179›Full record

ArticleJournal of bacteriology2006

Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ.

Katherine A Michie, Leigh G Monahan, Peter L Beech, Elizabeth J Harry

Abstract read
In one paragraph

Article in Journal of bacteriology, 2006. 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
–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

19 citing papers in PubMed.

  1. Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. Molecular Evolution of Tubulins in Diatoms.International journal of molecular sciences · 2022
    Article
  3. The bacterial divisome: ready for its close-up.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  4. Article
  5. Review
  6. Article
  7. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Microbiology and molecular biology reviews : MMBR · 2010
    Review
  8. Article
  9. Cellular polarity in prokaryotic organisms.Cold Spring Harbor perspectives in biology · 2009
    Review
  10. Article
  11. The dynamic nature of the bacterial cytoskeleton.Cellular and molecular life sciences : CMLS · 2009
    Review
  12. Review
  13. Modeling the physics of FtsZ assembly and force generation.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. Article
  16. Article
  17. The bacterial cytoskeleton.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  18. Review
  19. Article
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.

Katherine A MichieInstitute for the Biotechnology of Infectious Diseases, University of Technology, Sydney, NSW 2007, Australia.
Leigh G Monahan
Peter L Beech
Elizabeth J Harry

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The earliest stage in bacterial cell division is the formation of a ring, composed of the tubulin-like protein FtsZ, at the division site. Tight spatial and temporal regulation of Z-ring formation is required to ensure that division occurs precisely at midcell between two replicated chromosomes. However, the mechanism of Z-ring formation and its regulation in vivo remain unresolved. Here we identify the defect of an interesting temperature-sensitive ftsZ mutant (ts1) of Bacillus subtilis. At the nonpermissive temperature, the mutant protein, FtsZ(Ts1), assembles into spiral-like structures between chromosomes. When shifted back down to the permissive temperature, functional Z rings form and division resumes. Our observations support a model in which Z-ring formation at the division site arises from reorganization of a long cytoskeletal spiral form of FtsZ and suggest that the FtsZ(Ts1) protein is captured as a shorter spiral-forming intermediate that is unable to complete this reorganization step. The ts1 mutant is likely to be very valuable in revealing how FtsZ assembles into a ring and how this occurs precisely at the division site.

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsCell DivisionChromosomes, BacterialCytoskeletal ProteinsCytoskeletonModels, MolecularMolecular Sequence DataPoint MutationSequence AlignmentTemperatureBacterial ProteinsCytoskeletal ProteinsFtsZ protein, Bacteria

Identifiers

PMID16484179
PMCPMC1426551

What OpenQuestion holds

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Read underepoch 390

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.