Erskine_et_al-2018-Molecular_Microbiology.pdf (1.16 MB)
Formation of functional, non-amyloidogenic fibres by recombinant Bacillus subtilis TasA
Version 2 2023-06-12, 08:52
Version 1 2023-06-09, 13:08
journal contribution
posted on 2023-06-12, 08:52 authored by Elliot Erskine, Ryan J Morris, Marieke Schor, Chris Earl, Rachel M C Gillespie, Keith Bromley, Tetyana Sukhodub, Lauren Clark, Paul Fyfe, Louise SerpellLouise Serpell, Nicola R Stanley-Wall, Cait E MacPheeBacterial 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.
History
Publication status
- Published
File Version
- Published version
Journal
Molecular MicrobiologyISSN
0950-382XPublisher
WileyExternal DOI
Issue
6Volume
110Page range
897-913Department affiliated with
- Biochemistry Publications
Research groups affiliated with
- Dementia Research Group Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2018-05-03First Open Access (FOA) Date
2019-05-26First Compliant Deposit (FCD) Date
2018-05-03Usage metrics
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