The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV

Jessica L Hastie; Kyle B Williams; Craig D Ellermeier

doi:10.1128/JB.00292-13

Back

The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV

Journal article

Open access

Peer reviewed

The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV

Jessica L Hastie, Kyle B Williams and Craig D Ellermeier

Journal of bacteriology, Vol.195(14), pp.3135-3144

07/2013

DOI: 10.1128/JB.00292-13

PMCID: PMC3697642

PMID: 23687273

Files and links (1)

url

https://doi.org/10.1128/JB.00292-13View

Published (Version of record) Open Access

Abstract

During growth in the environment, bacteria encounter stresses which can delay or inhibit their growth. To defend against these stresses, bacteria induce both resistance and repair mechanisms. Many bacteria regulate these resistance mechanisms using a group of alternative σ factors called extracytoplasmic function (ECF) σ factors. ECF σ factors represent the largest and most diverse family of σ factors. Here, we demonstrate that the activation of a member of the ECF30 subfamily of ECF σ factors, σ(V) in Bacillus subtilis, is controlled by the proteolytic destruction of the anti-σ factor RsiV. We will demonstrate that the degradation of RsiV and, thus, the activation of σ(V) requires multiple proteolytic steps. Upon exposure to the inducer lysozyme, the extracellular domain of RsiV is removed by an unknown protease, which cleaves at site 1. This cleavage is independent of PrsW, the B. subtilis site 1 protease, which cleaves the anti-σ factor RsiW. Following cleavage by the unknown protease, the N-terminal portion of RsiV requires further processing, which requires the site 2 intramembrane protease RasP. Our data indicate that the N-terminal portion of RsiV from amino acid 1 to 60, which lacks the extracellular domain, is constitutively degraded unless RasP is absent, indicating that RasP cleavage is constitutive. This suggests that the regulatory step in RsiV degradation and, thus, σ(V) activation are controlled at the level of the site 1 cleavage. Finally, we provide evidence that increased resistance to lysozyme decreases σ(V) activation. Collectively, these data provide evidence that the mechanism for σ(V) activation in B. subtilis is controlled by regulated intramembrane proteolysis (RIP) and requires the site 2 protease RasP.

Sigma Factor - metabolism

Proteolysis

Bacterial Proteins - metabolism

Bacillus subtilis - enzymology

Muramidase - metabolism

Gene Expression Regulation, Bacterial

Bacillus subtilis - genetics

Peptide Hydrolases - metabolism

Details

Title: Subtitle: The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV
Creators: Jessica L Hastie - Department of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, IA, USA
Kyle B Williams
Craig D Ellermeier
Resource Type: Journal article
Publication Details: Journal of bacteriology, Vol.195(14), pp.3135-3144
DOI: 10.1128/JB.00292-13
PMID: 23687273
PMCID: PMC3697642
ISSN: 0021-9193
eISSN: 1098-5530
Grant note: R01 AI087834 / NIAID NIH HHS T32 AI007511 / NIAID NIH HHS R01AI087834 / NIAID NIH HHS
Language: English
Date published: 07/2013
Academic Unit: Microbiology and Immunology
Record Identifier: 9984083890802771

Metrics

8 Record Views

40 Times Cited - Web of Science