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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.
Original language | English |
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Article number | 6730 |
Pages (from-to) | 1-13 |
Number of pages | 13 |
Journal | Scientific Reports |
Volume | 7 |
DOIs | |
Publication status | Published - 27 Jul 2017 |
Keywords
- Biofilms
- Biological physics
- Supramolecular assembly
Fingerprint Dive into the research topics of 'Natural variations in the biofilm-associated protein BslA from the genus <i>Bacillus</i>'. Together they form a unique fingerprint.
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Student Theses
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Understanding the role of TapA in the formation of B. subtilis biofilms: a biochemical and genetic analysis
Author: Earl, C., 2018Supervisor: Stanley-Wall, N. (Supervisor) & Coulthurst, S. (Supervisor)
Student thesis: Doctoral Thesis › Doctor of Philosophy
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