Evidence map›Paper›PMID 21467045›Full record

ArticleThe Journal of biological chemistry2011

Bacterial tubulin distinct loop sequences and primitive assembly properties support its origin from a eukaryotic tubulin ancestor.

Antonio J Martin-Galiano, María A Oliva, Laura Sanz, Anamitra Bhattacharyya, Marina Serna, Hugo Yebenes, Jose M Valpuesta, Jose M Andreu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Nanoparticle-assisted tubulin assembly is environment dependent.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Archaea: A Goldmine for Molecular Biologists and Evolutionists.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  7. Review
  8. Review
  9. Article
  10. Four-stranded mini microtubules formed byProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. The bacterial cytoskeleton: more than twisted filaments.Current opinion in cell biology · 2013
    Review
  14. Archaeal origin of tubulin.Biology direct · 2012
    Article
  15. Article
  16. 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

8 authors at 4 institutions in 2 countries.

Antonio J Martin-GalianoCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
María A Oliva
Laura Sanz
Anamitra Bhattacharyya
Marina Serna
Hugo Yebenes
Jose M Valpuesta
Jose M Andreu
Centro de Investigaciones Biológicas Margarita Salas · ESConsejo Superior de Investigaciones Científicas · ESCentro Nacional de Biotecnología · ESIgenbio (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of the unique bacterial tubulin BtubA/B from Prosthecobacter is very similar to eukaryotic αβ-tubulin but, strikingly, BtubA/B fold without eukaryotic chaperones. Our sequence comparisons indicate that BtubA and BtubB do not really correspond to either α- or β-tubulin but have mosaic sequences with intertwining features from both. Their nucleotide-binding loops are more conserved, and their more divergent sequences correspond to discrete surface zones of tubulin involved in microtubule assembly and binding to eukaryotic cytosolic chaperonin, which is absent from the Prosthecobacter dejongeii draft genome. BtubA/B cooperatively assembles over a wider range of conditions than αβ-tubulin, forming pairs of protofilaments that coalesce into bundles instead of microtubules, and it lacks the ability to differentially interact with divalent cations and bind typical tubulin drugs. Assembled BtubA/B contain close to one bound GTP and GDP. Both BtubA and BtubB subunits hydrolyze GTP, leading to disassembly. The mutant BtubA/B-S144G in the tubulin signature motif GGG(T/S)G(S/T)G has strongly inhibited GTPase, but BtubA-T147G/B does not, suggesting that BtubB is a more active GTPase, like β-tubulin. BtubA/B chimera bearing the β-tubulin loops M, H1-S2, and S9-S10 in BtubB fold, assemble, and have reduced GTPase activity. However, introduction of the α-tubulin loop S9-S10 with its unique eight-residue insertion impaired folding. From the sequence analyses, its primitive assembly features, and the properties of the chimeras, we propose that BtubA/B were acquired shortly after duplication of a spontaneously folding α- and β-tubulin ancestor, possibly by horizontal gene transfer from a primitive eukaryotic cell, followed by divergent evolution.

Indexed as

Evolution, MolecularProtein FoldingAmino Acid SubstitutionBacterial ProteinsEukaryotic CellsGene Transfer, HorizontalGram-Negative BacteriaGuanosine DiphosphateGuanosine TriphosphateMutation, MissenseProtein Structure, SecondaryTubulinBacterial ProteinsGuanosine DiphosphateGuanosine TriphosphateTubulin

Identifiers

PMID21467045
PMCPMC3103357
OpenAlexW2042078404

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.