ArticlePLoS genetics2016
The Anti-sigma Factor RsiV Is a Bacterial Receptor for Lysozyme: Co-crystal Structure Determination and Demonstration That Binding of Lysozyme to RsiV Is Required for σV Activation.
Article in PLoS genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 32 citations in OpenAlex.
- Mixed positive and negative feedback loops drive diverse single-cell gene expression dynamics.Nature communications · 2026Article
- Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026Article
- Identification of DraRS inJournal of bacteriology · 2023Article
- The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.microLife · 2023Review
- The Cationic Antimicrobial Peptide Activity of Lysozyme Reduces ViableAntimicrobial agents and chemotherapy · 2022Article
- Activation of the Extracytoplasmic Function σ Factor σmSphere · 2022Article
- The WalR-WalK Signaling Pathway Modulates the Activities of both CwlO and LytE through Control of the Peptidoglycan Deacetylase PdaC in Bacillus subtilis.Journal of bacteriology · 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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- Effect of Lipidation on the Localization and Activity of a Lysozyme Inhibitor inJournal of bacteriology · 2020Article
- Changes in the expression of genes encoding type IV pili-associated proteins are seen when Clostridium perfringens is grown in liquid or on surfaces.BMC genomics · 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 σmSphere · 2019Article
- Deciphering the essentiality and function of the anti-σMolecular microbiology · 2019Article
- Activation of the extracytoplasmic function σ factor σMolecular microbiology · 2019Review
- Defining the regulon of genes controlled by σMolecular microbiology · 2019Article
- Screening Mycobacterium tuberculosis Secreted Proteins Identifies Mpt64 as a Eukaryotic Membrane-Binding Bacterial Effector.mSphere · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
σ factors provide RNA polymerase with promoter specificity in bacteria. Some σ factors require activation in order to interact with RNA polymerase and transcribe target genes. The Extra-Cytoplasmic Function (ECF) σ factor, σV, is encoded by several Gram-positive bacteria and is specifically activated by lysozyme. This activation requires the proteolytic destruction of the anti-σ factor RsiV via a process of regulated intramembrane proteolysis (RIP). In many cases proteases that cleave at site-1 are thought to directly sense a signal and initiate the RIP process. We previously suggested binding of lysozyme to RsiV initiated the proteolytic destruction of RsiV and activation of σV. Here we determined the X-ray crystal structure of the RsiV-lysozyme complex at 2.3 Å which revealed that RsiV and lysozyme make extensive contacts. We constructed RsiV mutants with altered abilities to bind lysozyme. We find that mutants that are unable to bind lysozyme block site-1 cleavage of RsiV and σV activation in response to lysozyme. Taken together these data demonstrate that RsiV is a receptor for lysozyme and binding of RsiV to lysozyme is required for σV activation. In addition, the co-structure revealed that RsiV binds to the lysozyme active site pocket. We provide evidence that in addition to acting as a sensor for the presence of lysozyme, RsiV also inhibits lysozyme activity. Thus we have demonstrated that RsiV is a protein with multiple functions. RsiV inhibits σV activity in the absence of lysozyme, RsiV binds lysozyme triggering σV activation and RsiV inhibits the enzymatic activity of lysozyme.
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