Tween 20 regulate the function and structure of transmembrane proteins of Bacillus cereus: Promoting transmembrane transport of fluoranthene

[Display omitted] •iTRAQ was used to study the function of transmembrane proteins.•Fluoranthene is transported by Bacillus cereus requiring protein and energy.•Tween 20 can improve the ability of Bacillus cereus to move.•Tween 20 can promotes the expression of specific transmembrane proteins.•The structure of transmembrane proteins involves α-helix and β-sheet interactions. Polycyclic aromatic hydrocarbons (PAHs) are degraded by the highly efficient degrading bacterium Bacillus cereus. Transmembrane transport is highly important in PAH degradation by bacteria. Surfactants are the key substances that promote PAH adsorption, uptake and transmembrane transport by Bacillus cereus. In this study, the isobaric tags for relative and absolute quantitation (iTRAQ) approach was used for high-throughput screening of key functional proteins during transmembrane fluoranthene transport by Bacillus cereus treated with Tween 20. In addition, SWISS-MODEL was used to simulate the tertiary structures of key transmembrane proteins and analyze how Tween 20 promotes transmembrane transport. Transmembrane fluoranthene transport into Bacillus cereus requires transmembrane proteins and energy. Tween 20 was observed to improve bacterial motility and transmembrane protein expression. The interior of representative transmembrane proteins is mostly composed of hydrophobic β-sheets while amphipathic α-helices are primarily distributed at their periphery. The primary reason for this configuration may be α-helices promote the aggregation of surfactants and the phospholipid bilayer and the β-sheets promote surfactant insertion into the phospholipid bilayer to enhance PAH transport into Bacillus cereus. Investigating the effect of Tween 20 on Bacillus cereus transmembrane proteins during transmembrane fluoranthene transport is important for understanding the mechanism of PAH degradation by microorganisms.