ArticleJournal of bacteriology2011
Effect of amino acid substitutions in the GerAA protein on the function of the alanine-responsive germinant receptor of Bacillus subtilis spores.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- GerAB residues predicted to interact with water based on MD simulations mediate germinosome stability inFrontiers in microbiology · 2026Article
- Recent progress in proteins regulating the germination ofJournal of bacteriology · 2025Review
- GerAB residues predicted to interfere with water passage based on steered molecular dynamics are key to germinosome functionality.Frontiers in microbiology · 2025Article
- Genomic identification of germinant receptors and phenotypic response to germinants inCurrent research in microbial sciences · 2025Article
- L-Alanine promotes anti-infectious properties of Bacillus subtilis S-2 spores via the germination receptor gerAA.Probiotics and antimicrobial proteins · 2024Article
- SpoVAF and FigP assemble into oligomeric ion channels that enhance spore germination.Genes & development · 2024Article
- Bacterial spore germination receptors are nutrient-gated ion channels.Science (New York, N.Y.) · 2023Article
- Genetic Suppression Meets Structure Prediction: Probing a Spore Germination Receptor Complex.Journal of bacteriology · 2022Article
- Genetic Evidence for Signal Transduction within the Bacillus subtilis GerA Germinant Receptor.Journal of bacteriology · 2022Article
- Dormant spores sense amino acids through the B subunits of their germination receptors.Nature communications · 2021Article
- Predicting the Structure and Dynamics of Membrane Protein GerAB fromInternational journal of molecular sciences · 2021Article
- Nutrient L-Alanine-Induced Germination ofFrontiers in microbiology · 2021Article
- Structural and functional analyses of the N-terminal domain of the A subunit of aProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Positions 299 and 302 of the GerAA subunit are important for function of the GerA spore germination receptor in Bacillus subtilis.PloS one · 2018Article
- Spore Heat Activation Requirements and Germination Responses Correlate with Sequences of Germinant Receptors and with the Presence of a SpecificApplied and environmental microbiology · 2017Article
- Analysis of Germination Capacity and Germinant Receptor (Sub)clusters of Genome-Sequenced Bacillus cereus Environmental Isolates and Model Strains.Applied and environmental microbiology · 2017Article
- Surviving Between Hosts: Sporulation and Transmission.Microbiology spectrum · 2016Review
- Article
- Monitoring of commitment, blocking, and continuation of nutrient germination of individual Bacillus subtilis spores.Journal of bacteriology · 2014Article
- L-alanine-induced germination in Bacillus licheniformis -the impact of native gerA sequences.BMC microbiology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spores of Bacillus subtilis require the GerAA, GerAB, and GerAC receptor proteins for L-alanine-induced germination. Mutations in gerAA, both random and site directed, result in phenotypes that identify amino acid residues important for receptor function in broad terms. They highlight the functional importance of two regions in the central, integral membrane domain of GerAA. A P324S substitution in the first residue of a conserved PFPP motif results in a 10-fold increase in a spore's sensitivity to alanine; a P326S change results in the release of phase-dark spores, in which the receptor may be in an "activated" or "quasigerminated" state. Substitutions in residues 398 to 400, in a short loop between the last two likely membrane-spanning helices of this central domain, all affect the germination response, with the G398S substitution causing a temperature-sensitive defect. In others, there are wider effects on the receptor: if alanine is substituted for conserved residue N146, H304, or E330, a severe defect in L-alanine germination results. This correlates with the absence of GerAC, suggesting that the assembly or stability of the entire receptor complex has been compromised by the defect in GerAA. In contrast, severely germination-defective mutants such as E129K, L373F, S400F, and M409N mutants retain GerAC at normal levels, suggesting more local and specific effects on the function of GerAA itself. Further interpretation will depend on progress in structural analysis of the receptor proteins.
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