Evidence map›Paper›PMID 21506936›Full record

ArticleThe Biochemical journal2011

Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding.

Abhrajyoti Ghosh, Sophia Hartung, Chris van der Does, John A Tainer, Sonja-Verena Albers

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
7.9field-weighted citation impact, top 3% 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

39 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. How Does the Archaellum Work?Biomolecules · 2025
    Review
  3. Article
  4. Article
  5. Membrane Adaptations and Cellular Responses ofInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Motile ghosts of the halophilic archaeon,Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  15. Review
  16. Article
  17. Motor torque measurement ofCommunications biology · 2019
    Article
  18. Taxis in archaea.Emerging topics in life sciences · 2018
    Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Abhrajyoti GhoshMolecular Biology of Archaea, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Strasse 10, 35043 Marburg, Germany.
Sophia Hartung
Chris van der Does
John A Tainer
Sonja-Verena Albers
Max Planck Institute for Terrestrial Microbiology · DE

Funding

Structure and Assembly of Type IV Pili &Related SystemsR01AI022160 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI TAINER, JOHN A. · 1985 to 2009
$3.2M
BIOPHYSICAL APPROACHES TO AMOEBIASISR01AI022106 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI LOEW, LESLIE M · 1985 to 1987
–
NIAID NIH HHS AI022106NIAID NIH HHS R01 AI022160
6 · The paper itself

Abstract

Microbial motility frequently depends on flagella or type IV pili. Using recently developed archaeal genetic tools, archaeal flagella and its assembly machinery have been identified. Archaeal flagella are functionally similar to bacterial flagella and their assembly systems are homologous with type IV pili assembly systems of Gram-negative bacteria. Therefore elucidating their biochemistry may result in insights in both archaea and bacteria. FlaI, a critical cytoplasmic component of the archaeal flagella assembly system in Sulfolobus acidocaldarius, is a member of the type II/IV secretion system ATPase superfamily, and is proposed to be bi-functional in driving flagella assembly and movement. In the present study we show that purified FlaI is a Mn2+-dependent ATPase that binds MANT-ATP [2'-/3'-O-(N'- methylanthraniloyl)adenosine-5'-O-triphosphate] with a high affinity and hydrolyses ATP in a co-operative manner. FlaI has an optimum pH and temperature of 6.5 and 75 °C for ATP hydrolysis. Remarkably, archaeal, but not bacterial, lipids stimulated the ATPase activity of FlaI 3-4-fold. Analytical gel filtration indicated that FlaI undergoes nucleotide-dependent oligomerization. Furthermore, SAXS (small-angle X-ray scattering) analysis revealed an ATP-dependent hexamerization of FlaI in solution. The results of the present study report the first detailed biochemical analyses of the motor protein of an archaeal flagellum.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateArchaeaArchaeal ProteinsBinding SitesFlagellaHydrogen-Ion ConcentrationLipid Metabolismortho-AminobenzoatesProtein FoldingTemperature3'-O-(N-methylanthraniloyl) ATPAdenosine TriphosphatasesAdenosine TriphosphateArchaeal Proteinsortho-Aminobenzoates

Identifiers

PMID21506936
PMCPMC3213642
OpenAlexW2064202871

What OpenQuestion holds

Textmetadata
LicenceTDM
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.