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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus amyloliquefaciens / genetics*
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Bacillus amyloliquefaciens / metabolism
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Bacillus licheniformis / genetics*
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Bacillus licheniformis / metabolism
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Bacillus pumilus / genetics*
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Bacillus pumilus / metabolism
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Bacillus subtilis / genetics*
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Bacillus subtilis / metabolism
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Biofilms / growth & development*
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Cloning, Molecular
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Elasticity
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression Regulation, Bacterial*
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Genetic Complementation Test
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Genetic Variation
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Genetic Vectors / chemistry
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Genetic Vectors / metabolism
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Hydrophobic and Hydrophilic Interactions
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Models, Molecular
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Phenotype
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Phylogeny
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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Recombinant Proteins