Interaction between type Ⅰ signal peptidase and signal peptides in Bacillus amyloliquefaciens
[Objective]Based on the critical role of type Ⅰ signal peptidase in the secretion system,this study explores the interaction between signal peptidase and signal peptides to guide the optimization of aminopeptidase secretion expression in Bacillus amyloliquefaciens.[Methods]The endogenous signal peptidase and signal peptide of Bacillus amyloliquefaciens TCCC 19030 were examined using relative fluorescence intensity and enzyme activity for analysis,and molecular docking to study their interaction.[Results]The signal peptide YolC fused with aminopeptidase exhibited the highest extracellular enzyme activity,reaching 11 847.67 U/mL.Overexpression of the signal peptidase SipW increased aminopeptidase activity to 16 261 U/mL.Molecular docking results also showed that YolC had the lowest binding free energy with SipW,at-4.4 kcal/mol.[Conclusion]Optimization of signal peptides and overexpression of signal peptidase can effectively enhance the secretion of aminopeptidase.The binding energy between signal peptidase and signal peptide is a key factor influencing the secretion levels of the target protein.
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