ArticleGenes & development2024
SpoVAF and FigP assemble into oligomeric ion channels that enhance spore germination.
Article in Genes & development, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- A mathematical kinetic model of memory iniScience · 2026Article
- Article
- Early activation of bioenergetic metabolism powers bacterial spore germination.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural and functional analysis ofMicrobiology (Reading, England) · 2025Article
- The Functional Network of PrkC and Its Interaction Proteins inMicroorganisms · 2025Article
- Germination ofJournal of bacteriology · 2025Article
- Recent progress in proteins regulating the germination ofJournal of bacteriology · 2025Review
- Newly identified SpoVAF/FigP complex: the role inApplied and environmental microbiology · 2025Article
- Identification and characterization of theJournal of bacteriology · 2024Article
- Spore germination: Two ion channels are better than one.Genes & development · 2024Article
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8 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial spores can remain dormant for decades yet rapidly germinate and resume growth in response to nutrients. GerA family receptors that sense and respond to these signals have recently been shown to oligomerize into nutrient-gated ion channels. Ion release initiates exit from dormancy. Here, we report that a distinct ion channel, composed of SpoVAF (5AF) and its newly discovered partner protein, YqhR (FigP), amplifies the response. At high germinant concentrations, 5AF/FigP accelerate germination; at low concentrations, this complex becomes critical for exit from dormancy. 5AF is homologous to the channel-forming subunit of GerA family receptors and is predicted to oligomerize around a central pore.
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