In-Depth Profiling of the LiaR Response of Bacillus subtilis
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The Lia system, a cell envelope stress response module of Bacillus subtilis, is comprised of the LiaRS two-component system and a membrane-anchored inhibitor protein, LiaF. It is highly conserved in the Firmicutes bacteria, and all orthologs investigated so far are activated by cell wall antibiotics. In response to envelope stress, the systems in Firmicutes cocci induce the expression of a number of genes that are involved in conferring resistance against its inducers. In contrast, a complete picture of the LiaR regulon of B. subtilis is still missing and no phenotypes could be associated with mutants lacking LiaRS. Here, we performed genome-wide transcriptomic, proteomic, and in-depth phenotypic profiling of constitutive “Lia ON” and “Lia OFF” mutants to obtain a comprehensive picture of the Lia response of Bacillus subtilis. In addition to the known targets liaIH and yhcYZ-yhdA, we identified ydhE as a novel gene affected by LiaR-dependent regulation. The results of detailed follow-up gene expression studies, together with proteomic analysis, demonstrate that the liaIH operon represents the only relevant LiaR target locus in vivo. It encodes a small membrane protein (LiaI) and a phage shock protein homolog (LiaH). LiaH forms large oligomeric rings reminiscent of those described for Escherichia coli PspA or Arabidopsis thaliana Vipp1. The results of comprehensive phenotype studies demonstrated that the gene products of the liaIH operon are involved in protecting the cell against oxidative stress and some cell wall antibiotics. Our data suggest that the LiaFSR system of B. subtilis and, presumably, other Firmicutes bacilli coordinates a phage shock protein-like response.
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Wolf et al. provided evidence indicating that liaIH is the only relevant target of LiaR-dependent gene expression in wild-type cells.
“Although LiaR regulates other genes, Wolf et al. provided evidence indicating that liaIH is the only relevant target of LiaR-dependent gene expression in wild-type cells.”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [93]
Expression of liaIH is completely LiaR-dependent.
“In contrast, expression of liaIH is completely LiaR-dependent.”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [93]
In B. subtilis, the lia locus consists of six genes, liaIH-liaGFSR, of which liaGFSR are constitutively expressed at a low basal level due to a weak constitutive promoter upstream of liaG.
“In B. subtilis, the lia locus consists of six genes, liaIH-liaGFSR, of which liaGFSR are constitutively expressed at a low basal level due to the presence of a weak constitutive promoter upstream of liaG.”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [93]
The LiaFSR system constitutes a cell envelope stress-sensing/response system that is highly conserved in Firmicutes bacteria.
“Importantly, the LiaFSR system constitutes a cell envelope stress-sensing/response system that is highly conserved in Firmicutes bacteria (93).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [93]
LiaI is a small hydrophobic protein of unknown function with two putative transmembrane helices and LiaH is a member of the phage-shock protein family that forms large oligomeric rings-like structures.
“LiaI is a small hydrophobic protein of unknown function with two putative transmembrane helices and LiaH is a member of the phage-shock protein family that forms large oligomeric rings-like structures (resembling what has been reported with PspA in E. coli).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [93]
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- Authors
- Wolf, D., Kalamorz, F., Wecke, T., Juszczak, A., Mäder, U., Homuth, G., Jordan, S., Kirstein, J., Hoppert, M., Voigt, B., Hecker, M., & Mascher, T.
- Affiliations
- Ludwig-Maximilians-Universität München (DE)
- University of Göttingen (DE)
- Interfaculty Institute for Genetics and Functional Genomics, Department for Functional Genomics, Ernst Moritz Arndt University, Greifswald, Germany
- Universität Greifswald (DE)
- Freie Universität Berlin (DE)
- Corresponding author
- Mascher, Thorsten
- ORCID
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2010-09-15
- Volume
- 192
- Issue
- 18
- Pages
- 4680-4693
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC2937411
- OpenAlex
- W2161167892
- Cited by
- 116
- References
- 63
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 7 · 2023: 3 · 2022: 4 · 2021: 6 · 2020: 13 · 2019: 3 · 2018: 1 · 2017: 5 · 2016: 15 · 2015: 12 · 2014: 8 · 2013: 6 · 2012: 11
- FWCI
- 4.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- GRO (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (MA2837/1-3, 03ZIK012)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- envelope stress response, oxidative stress resistance, Firmicutes, Bacillus subtilis, gene expression profiling, proteomics, phenotypic profiling
- MeSH terms
- Bacillus subtilis, Bacterial Proteins, Chromatography, Gel, Membrane Lipids, Promoter Regions, Genetic, Blotting, Northern, Electrophoresis, Gel, Two-Dimensional, Gene Expression Regulation, Bacterial, Polymerase Chain Reaction, Mutagenesis, Insertional, Sequence Deletion, Oligonucleotide Array Sequence Analysis, Microscopy, Electron, Transmission
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