Evidence map›Paper›PMID 22393043›Full record

ArticleThe Journal of biological chemistry2012

IcmF family protein TssM exhibits ATPase activity and energizes type VI secretion.

Lay-Sun Ma, Franz Narberhaus, Erh-Min Lai

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 1 pooled it
5.5field-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

48 citing papers in PubMed, 1 synthesis or guideline pooled it, 90 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Article
  3. Article
  4. mBio · 2025
    Article
  5. Article
  6. The role of type VI secretion system genes in antibiotic resistance and virulence inFrontiers in cellular and infection microbiology · 2024
    Article
  7. Protein-Protein Interactions: Co-immunoprecipitation.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Article
  9. Virulence genes identification inVeterinary world · 2023
    Article
  10. Type VI secretion system (T6SS) inIranian journal of microbiology · 2023
    Article
  11. Structure and Function of the Dot/Icm T4SS.bioRxiv : the preprint server for biology · 2023
    Article
  12. The type-VI secretion system of the beneficial symbiontMicrobiology (Reading, England) · 2023
    Review
  13. Uncovering the Secretion Systems ofAntibiotics (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Potential dsRNAs can be delivered to aquatic for defense pathogens.Frontiers in bioengineering and biotechnology · 2022
    Review
  18. 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

3 authors at 3 institutions in 2 countries.

Lay-Sun MaInstitute of Plant and Microbial Biology and the Molecular and Biological Agricultural Sciences Program, Taiwan International Graduate Program, Academia Sinica, Taipei 11529, Taiwan.
Franz Narberhaus
Erh-Min Lai
Institute of Plant and Microbial Biology, Academia Sinica · TWNational Chung Hsing University · TWRuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type VI secretion system (T6SS) with diversified functions is widely distributed in pathogenic Proteobacteria. The IcmF (intracellular multiplication protein F) family protein TssM is a conserved T6SS inner membrane protein. Despite the conservation of its Walker A nucleotide-binding motif, the NTPase activity of TssM and its role in T6SS remain obscure. In this study, we characterized TssM in the plant pathogen Agrobacterium tumefaciens and provided the first biochemical evidence for TssM exhibiting ATPase activity to power the secretion of the T6SS hallmark protein, hemolysin-coregulated protein (Hcp). Amino acid substitutions in the Walker A motif of TssM caused reduced ATP binding and hydrolysis activity. Importantly, we discovered the Walker B motif of TssM and demonstrated that it is critical for ATP hydrolysis activity. Protein-protein interaction studies and protease susceptibility assays indicated that TssM undergoes an ATP binding-induced conformational change and that subsequent ATP hydrolysis is crucial for recruiting Hcp to interact with the periplasmic domain of the TssM-interacting protein TssL (an IcmH/DotU family protein) into a ternary complex and mediating Hcp secretion. Our findings strongly argue that TssM functions as a T6SS energizer to recruit Hcp into the TssM-TssL inner membrane complex prior to Hcp secretion across the outer membrane.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAgrobacterium tumefaciensBacterial ProteinsCell MembraneHydrolysisImmunoblottingMembrane ProteinsModels, BiologicalMutationProtein BindingProtein TransportSpheroplastsAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsMembrane Proteins

Identifiers

PMID22393043
PMCPMC3346141
OpenAlexW2071464549

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.