Evidence map›Paper›PMID 23267091›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

ATP hydrolysis by a domain related to translation factor GTPases drives polymerization of a static bacterial morphogenetic protein.

Jean-Philippe Castaing, Attila Nagy, Vivek Anantharaman, L Aravind, Kumaran S Ramamurthi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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
2.7field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Interactions ofMicroorganisms · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. A 2-dimensional ratchet model describes assembly initiation of a specialized bacterial cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. SpoIVA-SipL Complex Formation Is Essential forJournal of bacteriology · 2019
    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 3 institutions in 1 country.

Jean-Philippe CastaingLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Attila Nagy
Vivek Anantharaman
L Aravind
Kumaran S Ramamurthi
National Cancer Institute · USNational Center for Biotechnology Information · USNational Heart Lung and Blood Institute · US

Funding

Subcellular protein localization in B. subtilisZIABC011211 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RAMAMURTHI, KUMARAN · 2009 to 2025
$21.4M
Evolutionary Analysis and Comparative Genomics of Protein SuperfamiliesZIALM594244 · NLM · NATIONAL LIBRARY OF MEDICINE · PI ARAVIND, L · 2009 to 2025
$20.3M
Intramural NIH HHS
6 · The paper itself

Abstract

The assembly of static supramolecular structures is a culminating event of developmental programs. One such structure, the proteinaceous shell (called the coat) that surrounds spores of the bacterium Bacillus subtilis, is composed of about 70 different proteins and represents one of the most durable biological structures known. The coat is built atop a basement layer that contains an ATPase (SpoIVA) that forms a platform required for coat assembly. Here, we show that SpoIVA belongs to the translation factors class of P-loop GTPases and has evolutionarily lost the ability to bind GTP; instead, it uses ATP hydrolysis to drive its self-assembly into static filaments. We demonstrate that ATP hydrolysis is required by every subunit for incorporation into the growing polymer by inducing a conformational change that drives polymerization of a nucleotide-free filament. SpoIVA therefore differs from other self-organizing polymers (dynamic cytoskeletal structures and static intermediate filaments) in that it uses ATP hydrolysis to self-assemble, not disassemble, into a static polymer. We further show that polymerization requires a critical concentration that we propose is only achieved once SpoIVA is recruited to the surface of the developing spore, thereby ensuring that SpoIVA polymerization only occurs at the correct subcellular location during spore morphogenesis.

Indexed as

Models, MolecularAdenosine TriphosphateBacillus subtilisBacterial ProteinsComputational BiologyGTP PhosphohydrolasesHydrolysisLikelihood FunctionsMicroscopy, FluorescenceModels, GeneticPhylogenyPolymerizationProtein ConformationSpores, BacterialAdenosine TriphosphateBacterial ProteinsGTP Phosphohydrolasesspore-specific proteins, Bacillus

Identifiers

PMID23267091
PMCPMC3545789
OpenAlexW2091013376

What OpenQuestion holds

Textmetadata
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.