Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-Ïƒ factor RsiV controls activation of the ecf Ïƒ factor ÏƒV

Jessica L Hastie; Kyle B Williams; Carolina Sepúlveda; Jon C Houtman; Katrina T Forest; Craig D Ellermeier

doi:10.1371/journal.pgen.1004643

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Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-Ïƒ factor RsiV controls activation of the ecf Ïƒ factor ÏƒV

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Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-Ïƒ factor RsiV controls activation of the ecf Ïƒ factor ÏƒV

Jessica L Hastie, Kyle B Williams, Carolina Sepúlveda, Jon C Houtman, Katrina T Forest and Craig D Ellermeier

PLoS genetics, Vol.10(10), pp.e1004643-e1004643

10/2014

DOI: 10.1371/journal.pgen.1004643

PMCID: PMC4183432

PMID: 25275625

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Abstract

σ factors endow RNA polymerase with promoter specificity in bacteria. Extra-Cytoplasmic Function (ECF) σ factors represent the largest and most diverse family of σ factors. Most ECF σ factors must be activated in response to an external signal. One mechanism of activation is the stepwise proteolytic destruction of an anti-σ factor via Regulated Intramembrane Proteolysis (RIP). In most cases, the site-1 protease required to initiate the RIP process directly senses the signal. Here we report a new mechanism in which the anti-σ factor rather than the site-1 protease is the sensor. We provide evidence suggesting that the anti-σ factor RsiV is the bacterial receptor for the innate immune defense enzyme, lysozyme. The site-1 cleavage site is similar to the recognition site of signal peptidase and cleavage at this site is required for σV activation in Bacillus subtilis. We reconstitute site-1 cleavage in vitro and demonstrate that it requires both signal peptidase and lysozyme. We demonstrate that the anti-σ factor RsiV directly binds to lysozyme and muramidase activity is not required for σV activation. We propose a model in which the binding of lysozyme to RsiV activates RsiV for signal peptidase cleavage at site-1, initiating proteolytic destruction of RsiV and activation of σV. This suggests a novel mechanism in which conformational change in a substrate controls the cleavage susceptibility for signal peptidase. Thus, unlike other ECF σ factors which require regulated intramembrane proteolysis for activation, the sensor for σV activation is not the site-1 protease but the anti-σ factor.

Endopeptidases - metabolism

Sigma Factor - metabolism

Membrane Proteins - genetics

Muramidase - genetics

Proprotein Convertases - metabolism

Bacterial Proteins - genetics

Muramidase - metabolism

Proprotein Convertases - genetics

Bacillus subtilis - genetics

Calorimetry - methods

Clostridioides difficile - metabolism

Enterococcus faecalis - metabolism

Serine Endopeptidases - genetics

Bacterial Proteins - metabolism

Membrane Proteins - metabolism

Serine Endopeptidases - metabolism

Gene Expression Regulation, Bacterial

Sigma Factor - genetics

Bacillus subtilis - metabolism

Details

Title: Subtitle: Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-Ïƒ factor RsiV controls activation of the ecf Ïƒ factor ÏƒV
Creators: Jessica L Hastie - Department of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America
Kyle B Williams - Department of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America
Carolina Sepúlveda - Department of Bacteriology, University of Wisconsin Madison, Madison, Wisconsin, United States of America
Jon C Houtman - Department of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America
Katrina T Forest - Department of Bacteriology, University of Wisconsin Madison, Madison, Wisconsin, United States of America
Craig D Ellermeier - Department of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America
Resource Type: Journal article
Publication Details: PLoS genetics, Vol.10(10), pp.e1004643-e1004643
DOI: 10.1371/journal.pgen.1004643
PMID: 25275625
PMCID: PMC4183432
NLM abbreviation: PLoS Genet
ISSN: 1553-7390
eISSN: 1553-7404
Publisher: Public Library Science
Grant note: T32 AI007511 / NIAID NIH HHS R01 AI087834 / NIAID NIH HHS T32 AI07511 / NIAID NIH HHS R01AI087834 / NIAID NIH HHS
Language: English
Date published: 10/2014
Academic Unit: Microbiology and Immunology; Internal Medicine
Record Identifier: 9984083871802771

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