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Published on: December 29, 2023
Activation of the extracytoplasmic function σ factor σV by lysozyme
Theresa D Ho1, Craig D Ellermeier1,2
1Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 431 Newton Rd, Iowa City, IA, 52242, USA.
Sigma V (σV) is activated by lysozyme in Firmicutes bacteria, enabling resistance. This occurs when lysozyme binding triggers the degradation of its inhibitor, RsiV, via a unique signal peptidase cleavage mechanism.
Area of Science:
- Microbiology
- Bacterial Physiology
- Signal Transduction
Background:
- Sigma V (σV) is an extracytoplasmic function (ECF) σ factor found in Firmicutes, crucial for lysozyme resistance.
- Its activity is regulated by the anti-σ factor RsiV, a transmembrane protein that also acts as a lysozyme receptor.
Purpose of the Study:
- To elucidate the mechanism of σV activation in response to lysozyme.
- To investigate the role of RsiV degradation in the activation cascade.
Main Methods:
- Analysis of the RsiV degradation pathway.
- Identification of the protease responsible for site-1 cleavage of RsiV.
- Lysozyme-dependent assays to study RsiV cleavage and σV activation.
Main Results:
- Lysozyme binding to RsiV initiates a signal transduction cascade leading to RsiV degradation.
- Site-1 cleavage of RsiV is performed by a constitutively active signal peptidase in a lysozyme-dependent manner.
- Activated σV drives the transcription of genes essential for lysozyme resistance.
Conclusions:
- The σV-RsiV system provides a specific mechanism for lysozyme resistance in Firmicutes.
- Signal peptidase plays a unique, lysozyme-regulated role in activating ECF σ factors.
- Understanding this pathway offers insights into bacterial defense mechanisms against cell wall-degrading enzymes.
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