Evidence map›Paper›PMID 22162949›Full record

ArticlePLoS biology2011

Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.

Martin Pilhofer, Mark S Ladinsky, Alasdair W McDowall, Giulio Petroni, Grant J Jensen

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Nanoparticle-assisted tubulin assembly is environment dependent.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
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  9. Article
  10. Virus-Induced Membrane Fusion in Neurodegenerative Disorders.Frontiers in cellular and infection microbiology · 2022
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Nonlinear Elastic and Inelastic Properties of Cells.Journal of biomechanical engineering · 2020
    Review
  18. Review
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Martin PilhoferCalifornia Institute of Technology, Pasadena, California, USA. martin-pilhofer@web.de
Mark S Ladinsky
Alasdair W McDowall
Giulio Petroni
Grant J Jensen
California Institute of Technology · USUniversity of Pisa · IT

Funding

Structure and function of the prokaryotic cytoskeleton by electron cryotomographyR01GM094800 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI JENSEN, GRANT J · 2011 to 2015
$1.7M
NIGMS NIH HHS R01 GM094800NIGMS NIH HHS R01 GM094800B
6 · The paper itself

Abstract

Microtubules play crucial roles in cytokinesis, transport, and motility, and are therefore superb targets for anti-cancer drugs. All tubulins evolved from a common ancestor they share with the distantly related bacterial cell division protein FtsZ, but while eukaryotic tubulins evolved into highly conserved microtubule-forming heterodimers, bacterial FtsZ presumably continued to function as single homopolymeric protofilaments as it does today. Microtubules have not previously been found in bacteria, and we lack insight into their evolution from the tubulin/FtsZ ancestor. Using electron cryomicroscopy, here we show that the tubulin homologs BtubA and BtubB form microtubules in bacteria and suggest these be referred to as "bacterial microtubules" (bMTs). bMTs share important features with their eukaryotic counterparts, such as straight protofilaments and similar protofilament interactions. bMTs are composed of only five protofilaments, however, instead of the 13 typical in eukaryotes. These and other results suggest that rather than being derived from modern eukaryotic tubulin, BtubA and BtubB arose from early tubulin intermediates that formed small microtubules. Since we show that bacterial microtubules can be produced in abundance in vitro without chaperones, they should be useful tools for tubulin research and drug screening.

Indexed as

Bacterial ProteinsCryoelectron MicroscopyCytoskeletal ProteinsCytoskeletonGene ExpressionPhylogenyRecombinant ProteinsRNA, MessengerTubulinVerrucomicrobiaBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaRecombinant ProteinsRNA, MessengerTubulin

Identifiers

PMID22162949
PMCPMC3232192
OpenAlexW2166914530

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.