ArticlePLoS genetics2018
Bacterial sensing: A putative amphipathic helix in RsiV is the switch for activating σV in response to lysozyme.
Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- Mixed positive and negative feedback loops drive diverse single-cell gene expression dynamics.Nature communications · 2026Article
- Identification of a family of peptidoglycan transpeptidases reveals thatProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification of DraRS inJournal of bacteriology · 2023Article
- Activation of the Extracytoplasmic Function σ Factor σmSphere · 2022Article
- Activation of the extracytoplasmic function σ factor σCurrent opinion in microbiology · 2022Review
- SigV Mediates Lysozyme Resistance in Enterococcus faecalis via RsiV and PgdA.Journal of bacteriology · 2021Article
- Tunable phenotypic variability through an autoregulatory alternative sigma factor circuit.Molecular systems biology · 2021Article
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- Holin-Dependent Secretion of the Large Clostridial Toxin TpeL by Clostridium perfringens.Journal of bacteriology · 2021Article
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- Effect of Lipidation on the Localization and Activity of a Lysozyme Inhibitor inJournal of bacteriology · 2020Article
- Role of Regulated Proteolysis in the Communication of Bacteria With the Environment.Frontiers in molecular biosciences · 2020Review
- Activation of the extracytoplasmic function σ factor σMolecular microbiology · 2019Review
- Defining the regulon of genes controlled by σMolecular microbiology · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Extra Cytoplasmic Function (ECF) σ factors are a diverse group of alternate σ factors bacteria use to respond to changes in the environment. The Bacillus subtilis ECF σ factor σV responds to lysozyme. In the absence of lysozyme, σV is held inactive by the anti-σ factor, RsiV. In the presence of lysozyme RsiV is degraded via regulated intramembrane proteolysis, which results in the release of σV and thus activation of lysozyme resistance genes. Signal peptidase is required to initiate degradation of RsiV. Previous work indicated that RsiV only becomes sensitive to signal peptidase upon direct binding to lysozyme. We have identified a unique domain of RsiV that is responsible for protecting RsiV from cleavage by signal peptidase in the absence of lysozyme. We provide evidence that this domain contains putative amphipathic helices. Disruption of the hydrophobic surface of these helices by introducing positively charged residues results in constitutive cleavage of RsiV by signal peptidase and thus constitutive σV activation. We provide further evidence that this domain contains amphipathic helices using a membrane-impermeable reagent. Finally, we show that upon lysozyme binding to RsiV, the hydrophobic face of the amphipathic helix becomes accessible to a membrane-impermeable reagent. Thus, we propose the amphipathic helices protect RsiV from cleavage in the absence of lysozyme. Additionally, we propose the amphipathic helices rearrange to form a suitable signal peptidase substrate upon binding of RsiV to lysozyme leading to the activation of σV.
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