LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 5 of total 5

Search options

  1. Article ; Online: The putative role of the epipeptide EpeX in

    Kalamara, Margarita / Abbott, James / Sukhodub, Tetyana / MacPhee, Cait / Stanley-Wall, Nicola R

    Microbiology (Reading, England)

    2023  Volume 169, Issue 6

    Abstract: Bacteria engage in competitive interactions with neighbours that can either be of the same or different species. Multiple mechanisms are deployed to ensure the desired outcome and one tactic commonly implemented is the production of specialised ... ...

    Abstract Bacteria engage in competitive interactions with neighbours that can either be of the same or different species. Multiple mechanisms are deployed to ensure the desired outcome and one tactic commonly implemented is the production of specialised metabolites. The Gram-positive bacterium
    MeSH term(s) Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Biofilms
    Language English
    Publishing date 2023-05-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1180712-x
    ISSN 1465-2080 ; 1350-0872
    ISSN (online) 1465-2080
    ISSN 1350-0872
    DOI 10.1099/mic.0.001344
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article ; Online: The majority of the matrix protein TapA is dispensable for Bacillus subtilis colony biofilm architecture.

    Earl, Chris / Arnaouteli, Sofia / Bamford, Natalie C / Porter, Michael / Sukhodub, Tetyana / MacPhee, Cait E / Stanley-Wall, Nicola R

    Molecular microbiology

    2020  Volume 114, Issue 6, Page(s) 920–933

    Abstract: Biofilm formation is a co-operative behaviour, where microbial cells become embedded in an extracellular matrix. This biomolecular matrix helps manifest the beneficial or detrimental outcome mediated by the collective of cells. Bacillus subtilis is an ... ...

    Abstract Biofilm formation is a co-operative behaviour, where microbial cells become embedded in an extracellular matrix. This biomolecular matrix helps manifest the beneficial or detrimental outcome mediated by the collective of cells. Bacillus subtilis is an important bacterium for understanding the principles of biofilm formation. The protein components of the B. subtilis matrix include the secreted proteins BslA, which forms a hydrophobic coat over the biofilm, and TasA, which forms protease-resistant fibres needed for structuring. TapA is a secreted protein also needed for biofilm formation and helps in vivo TasA-fibre formation but is dispensable for in vitro TasA-fibre assembly. We show that TapA is subjected to proteolytic cleavage in the colony biofilm and that only the first 57 amino acids of the 253-amino acid protein are required for colony biofilm architecture. Through the construction of a strain which lacks all eight extracellular proteases, we show that proteolytic cleavage by these enzymes is not a prerequisite for TapA function. It remains unknown why TapA is synthesised at 253 amino acids when the first 57 are sufficient for colony biofilm structuring; the findings do not exclude the core conserved region of TapA having a second role beyond structuring the B. subtilis colony biofilm.
    MeSH term(s) Amino Acid Sequence ; Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacillus subtilis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms/growth & development ; Extracellular Matrix Proteins/genetics ; Extracellular Matrix Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Sequence Deletion
    Chemical Substances Bacterial Proteins ; Extracellular Matrix Proteins
    Language English
    Publishing date 2020-06-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.14559
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: Formation of functional, non-amyloidogenic fibres by recombinant Bacillus subtilis TasA.

    Erskine, Elliot / Morris, Ryan J / Schor, Marieke / Earl, Chris / Gillespie, Rachel M C / Bromley, Keith M / Sukhodub, Tetyana / Clark, Lauren / Fyfe, Paul K / Serpell, Louise C / Stanley-Wall, Nicola R / MacPhee, Cait E

    Molecular microbiology

    2018  Volume 110, Issue 6, Page(s) 897–913

    Abstract: Bacterial biofilms are communities of microbial cells encased within a self-produced polymeric matrix. In the Bacillus subtilis biofilm matrix, the extracellular fibres of TasA are essential. Here, a recombinant expression system allows interrogation of ... ...

    Abstract Bacterial biofilms are communities of microbial cells encased within a self-produced polymeric matrix. In the Bacillus subtilis biofilm matrix, the extracellular fibres of TasA are essential. Here, a recombinant expression system allows interrogation of TasA, revealing that monomeric and fibre forms of TasA have identical secondary structure, suggesting that fibrous TasA is a linear assembly of globular units. Recombinant TasA fibres form spontaneously, and share the biological activity of TasA fibres extracted from B. subtilis, whereas a TasA variant restricted to a monomeric form is inactive and subjected to extracellular proteolysis. The biophysical properties of both native and recombinant TasA fibres indicate that they are not functional amyloid-like fibres. A gel formed by TasA fibres can recover after physical shear force, suggesting that the biofilm matrix is not static and that these properties may enable B. subtilis to remodel its local environment in response to external cues. Using recombinant fibres formed by TasA orthologues we uncover species variability in the ability of heterologous fibres to cross-complement the B. subtilis tasA deletion. These findings are indicative of specificity in the biophysical requirements of the TasA fibres across different species and/or reflect the precise molecular interactions needed for biofilm matrix assembly.
    MeSH term(s) Amyloidogenic Proteins/chemistry ; Amyloidogenic Proteins/genetics ; Amyloidogenic Proteins/metabolism ; Bacillus subtilis/metabolism ; Bacillus subtilis/physiology ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
    Chemical Substances Amyloidogenic Proteins ; Bacterial Proteins ; Recombinant Proteins ; TasA protein, Bacillus subtilis
    Language English
    Publishing date 2018-11-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.13985
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article ; Online: Natural variations in the biofilm-associated protein BslA from the genus Bacillus.

    Morris, Ryan J / Schor, Marieke / Gillespie, Rachel M C / Ferreira, Ana Sofia / Baldauf, Lucia / Earl, Chris / Ostrowski, Adam / Hobley, Laura / Bromley, Keith M / Sukhodub, Tetyana / Arnaouteli, Sofia / Stanley-Wall, Nicola R / MacPhee, Cait E

    Scientific reports

    2017  Volume 7, Issue 1, Page(s) 6730

    Abstract: BslA is a protein secreted by Bacillus subtilis which forms a hydrophobic film that coats the biofilm surface and renders it water-repellent. We have characterised three orthologues of BslA from Bacillus amyloliquefaciens, Bacillus licheniformis and ... ...

    Abstract BslA is a protein secreted by Bacillus subtilis which forms a hydrophobic film that coats the biofilm surface and renders it water-repellent. We have characterised three orthologues of BslA from Bacillus amyloliquefaciens, Bacillus licheniformis and Bacillus pumilus as well as a paralogue from B. subtilis called YweA. We find that the three orthologous proteins can substitute for BslA in B. subtilis and confer a degree of protection, whereas YweA cannot. The degree to which the proteins functionally substitute for native BslA correlates with their in vitro biophysical properties. Our results demonstrate the use of naturally-evolved variants to provide a framework for teasing out the molecular basis of interfacial self-assembly.
    MeSH term(s) Amino Acid Sequence ; Bacillus amyloliquefaciens/genetics ; Bacillus amyloliquefaciens/metabolism ; Bacillus licheniformis/genetics ; Bacillus licheniformis/metabolism ; Bacillus pumilus/genetics ; Bacillus pumilus/metabolism ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms/growth & development ; Cloning, Molecular ; Elasticity ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression Regulation, Bacterial ; Genetic Complementation Test ; Genetic Variation ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Phenotype ; Phylogeny ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid
    Chemical Substances Bacterial Proteins ; Recombinant Proteins
    Language English
    Publishing date 2017-07-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-017-06786-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article ; Online: Bifunctionality of a biofilm matrix protein controlled by redox state.

    Arnaouteli, Sofia / Ferreira, Ana Sofia / Schor, Marieke / Morris, Ryan J / Bromley, Keith M / Jo, Jeanyoung / Cortez, Krista L / Sukhodub, Tetyana / Prescott, Alan R / Dietrich, Lars E P / MacPhee, Cait E / Stanley-Wall, Nicola R

    Proceedings of the National Academy of Sciences of the United States of America

    2017  Volume 114, Issue 30, Page(s) E6184–E6191

    Abstract: Biofilms are communities of microbial cells that are encapsulated within a self-produced polymeric matrix. The matrix is critical to the success of biofilms in diverse habitats; however, many details of the composition, structure, and function remain ... ...

    Abstract Biofilms are communities of microbial cells that are encapsulated within a self-produced polymeric matrix. The matrix is critical to the success of biofilms in diverse habitats; however, many details of the composition, structure, and function remain enigmatic. Biofilms formed by the Gram-positive bacterium
    MeSH term(s) Bacillus subtilis/genetics ; Bacillus subtilis/physiology ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Bacterial Proteins/physiology ; Biofilms ; Hydrophobic and Hydrophilic Interactions ; Oxidation-Reduction
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2017-07-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1707687114
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top