Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA.

ABSTRACT: The soil bacterium Bacillus subtilis is a model organism to investigate the formation of biofilms, the predominant form of microbial life. The secreted protein BslA self-assembles at the surface of the biofilm to give the B. subtilis biofilm its characteristic hydrophobicity. To understand the mechanism of BslA self-assembly at interfaces, here we built a molecular model based on the previous BslA crystal structure and the crystal structure of the BslA paralogue YweA that we determined. Our analysis revealed two conserved protein-protein interaction interfaces supporting BslA self-assembly into an infinite 2-dimensional lattice that fits previously determined transmission microscopy images. Molecular dynamics simulations and in vitro protein assays further support our model o

SUBMITTER: Arnaouteli S 

PROVIDER: S-EPMC7615278 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature