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Dual functionality of the amyloid protein TasA in Bacillus physiology and fitness on the phylloplane
- Source :
- Nature Communications, Nature Communications, Vol 11, Iss 1, Pp 1-21 (2020)
- Publication Year :
- 2020
-
Abstract
- Bacteria can form biofilms that consist of multicellular communities embedded in an extracellular matrix (ECM). In Bacillus subtilis, the main protein component of the ECM is the functional amyloid TasA. Here, we study further the roles played by TasA in B. subtilis physiology and biofilm formation on plant leaves and in vitro. We show that ΔtasA cells exhibit a range of cytological symptoms indicative of excessive cellular stress leading to increased cell death. TasA associates to the detergent-resistant fraction of the cell membrane, and the distribution of the flotillin-like protein FloT is altered in ΔtasA cells. We propose that, in addition to a structural function during ECM assembly and interactions with plants, TasA contributes to the stabilization of membrane dynamics as cells enter stationary phase.<br />The amyloid protein TasA is a main component of the extracellular matrix in Bacillus subtilis biofilms. Here the authors show that, in addition to a structural function during biofilm assembly and interactions with plants, TasA contributes to the stabilization of membrane dynamics during stationary phase.
- Subjects :
- 0301 basic medicine
Organisms::Bacteria::Gram-Positive Bacteria::Bacillales::Bacillaceae::Bacillus::Bacillus subtilis [Medical Subject Headings]
General Physics and Astronomy
Physiology
Bacillus
Bacillus subtilis
Amyloidogenic proteins
Organisms::Bacteria::Gram-Positive Bacteria::Bacillales::Bacillaceae::Bacillus [Medical Subject Headings]
Bacterial Adhesion
Microbial ecology
Extracellular matrix
Cell membrane
Disciplines and Occupations::Natural Science Disciplines::Biological Science Disciplines::Biology::Ecology [Medical Subject Headings]
Bacterial proteins
Proteínas amiloidogénicas
lcsh:Science
Multidisciplinary
Cell Death
Ecology
biology
Membrana celular
Chemistry
Chemicals and Drugs::Amino Acids, Peptides, and Proteins::Proteins::Amyloid::Amyloidogenic Proteins [Medical Subject Headings]
Chemicals and Drugs::Lipids::Lipopeptides [Medical Subject Headings]
medicine.anatomical_structure
Organisms::Eukaryota::Plants::Viridiplantae::Streptophyta::Embryophyta::Angiosperms::Cucurbitaceae [Medical Subject Headings]
Bacterias
Cell death
Phenomena and Processes::Microbiological Phenomena::Biofilms [Medical Subject Headings]
Programmed cell death
Phenomena and Processes::Genetic Phenomena::Genetic Variation::Mutation [Medical Subject Headings]
Amyloid
Chemicals and Drugs::Amino Acids, Peptides, and Proteins::Proteins::Bacterial Proteins [Medical Subject Headings]
Science
Phenomena and Processes::Genetic Phenomena::Genetic Processes::Gene Expression::Transcription, Genetic::Transcriptome [Medical Subject Headings]
030106 microbiology
Bacterial adhesion
Amyloidogenic Proteins
Article
General Biochemistry, Genetics and Molecular Biology
Lipopeptides
03 medical and health sciences
Bacterial Proteins
medicine
Cellular microbiology
Anatomy::Cells::Cellular Structures::Cell Membrane [Medical Subject Headings]
Phenomena and Processes::Microbiological Phenomena::Bacterial Physiological Phenomena::Bacterial Processes::Bacterial Adhesion [Medical Subject Headings]
Bacteria
Cell Membrane
fungi
Biofilm
General Chemistry
biochemical phenomena, metabolism, and nutrition
Phenomena and Processes::Cell Physiological Phenomena::Cell Physiological Processes::Cell Death [Medical Subject Headings]
biology.organism_classification
Muerte celular
Cucurbitaceae
Proteínas bacterianas
030104 developmental biology
Biofilms
Tasa
Mutation
lcsh:Q
Transcriptome
Function (biology)
Subjects
Details
- ISSN :
- 20411723
- Database :
- OpenAIRE
- Journal :
- Nature Communications
- Accession number :
- edsair.doi.dedup.....6eaee10ce20d546f1feb0d53d9f55b63
- Full Text :
- https://doi.org/10.1038/s41467-020-15758-z