Evidence map›Paper›PMID 24706863›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Medicago truncatula symbiotic peptide NCR247 contributes to bacteroid differentiation through multiple mechanisms.

Attila Farkas, Gergely Maróti, Hajnalka Durgő, Zoltán Györgypál, Rui M Lima, Katalin F Medzihradszky, Attila Kereszt, Peter Mergaert, Éva Kondorosi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
24.3field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 178 citations in OpenAlex.

  1. Article
  2. Article
  3. BacA(SbmA) importer of legume symbiotic NCR peptides: Protein architecture, function, and evolutionary implications.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  12. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. A microaerobically induced small heat shock protein contributes toApplied and environmental microbiology · 2025
    Article
  15. Review
  16. Review
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  18. Article
  19. TheJournal of bacteriology · 2024
    Article
  20. Article

28 more citing papers are in PubMed but not listed here.

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

9 authors at 4 institutions in 2 countries.

Attila FarkasInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, 6726, Szeged, Hungary.
Gergely Maróti
Hajnalka Durgő
Zoltán Györgypál
Rui M Lima
Katalin F Medzihradszky
Attila Kereszt
Peter Mergaert
Éva Kondorosi
HUN-REN Szegedi Biológiai Kutatóközpont · HUInstitute of Biochemistry · HUHungarian Academy of Sciences · HUInstitut des Sciences du Végétal · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Symbiosis between rhizobia soil bacteria and legume plants results in the formation of root nodules where plant cells are fully packed with nitrogen fixing bacteria. In the host cells, the bacteria adapt to the intracellular environment and gain the ability for nitrogen fixation. Depending on the host plants, the symbiotic fate of bacteria can be either reversible or irreversible. In Medicago and related legume species, the bacteria undergo a host-directed multistep differentiation process culminating in the formation of elongated and branched polyploid bacteria with definitive loss of cell division ability. The plant factors are nodule-specific symbiotic peptides. Approximately 600 of them are nodule-specific cysteine-rich (NCR) peptides produced in the rhizobium-infected plant cells. NCRs are targeted to the endosymbionts, and concerted action of different sets of peptides governs different stages of endosymbiont maturation, whereas the symbiotic function of individual NCRs is unknown. This study focused on NCR247, a cationic peptide exhibiting in vitro antimicrobial activities. We show that NCR247 acts in those nodule cells where bacterial cell division is arrested and cell elongation begins. NCR247 penetrates the bacteria and forms complexes with many bacterial proteins. Interaction with FtsZ required for septum formation is one of the host interventions for inhibiting bacterial cell division. Complex formation with the ribosomal proteins affects translation and contributes to altered proteome and physiology of the endosymbiont. Binding to the chaperone GroEL amplifies the NCR247-modulated biological processes. We show that GroEL1 of Sinorhizobium meliloti is required for efficient infection, terminal differentiation, and nitrogen fixation.

Indexed as

SymbiosisAnti-Bacterial AgentsBacteriaBacterial ProteinsMedicago truncatulaNitrogen FixationPeptidesPlant ProteinsProtein BindingAnti-Bacterial AgentsBacterial ProteinsPeptidesPlant Proteinsantimicrobial peptidesbacterial targetshost peptidesprotein interactionstranslation inhibition

Identifiers

PMID24706863
PMCPMC3986156
OpenAlexW1991181361

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.