ArticleMicrobial cell factories2017
A novel strategy to improve protein secretion via overexpression of the SppA signal peptide peptidase in Bacillus licheniformis.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 48 citations in OpenAlex.
- The Construction of an Environmentally Friendly Super-Secreting Strain ofInternational journal of molecular sciences · 2024Article
- Review
- Advances in recombinant protease production: current state and perspectives.World journal of microbiology & biotechnology · 2024Review
- Designing a conjugate vaccine targetingHeliyon · 2024Article
- The ins and outs of Bacillus proteases: activities, functions and commercial significance.FEMS microbiology reviews · 2022Review
- ProbioticApplied and environmental microbiology · 2021Article
- Optimization, Characteristics, and Functions of Alkaline Phosphatase FromFrontiers in microbiology · 2021Article
- SppI Forms a Membrane Protein Complex with SppA and Inhibits Its Protease Activity in Bacillus subtilis.mSphere · 2020Article
- Construction of a High-Expression System in Bacillus through Transcriptomic Profiling and Promoter Engineering.Microorganisms · 2020Article
- Translational regulation of periplasmic folding assistants and proteases as a valuable strategy to improve production of translocated recombinant proteins in Escherichia coli.BMC biotechnology · 2020Article
- Cloning, Prokaryotic Soluble Expression, and Analysis of Antiviral Activity of Two Novel Feline IFN-ω Proteins.Viruses · 2020Article
- Enhanced Bacitracin Production by Systematically Engineering S-Adenosylmethionine Supply Modules inFrontiers in bioengineering and biotechnology · 2020Article
- Enhanced production of heterologous proteins via engineering the cell surface of Bacillus licheniformis.Journal of industrial microbiology & biotechnology · 2019Article
- Improved the expression level of active transglutaminase by directional increasing copy of mtg gene in Pichia pastoris.BMC biotechnology · 2019Article
- Enhancement of precursor amino acid supplies for improving bacitracin production by activation of branched chain amino acid transporter BrnQ and deletion of its regulator geneSynthetic and systems biotechnology · 2018Article
- Exploitation of Bacillus subtilis as a robust workhorse for production of heterologous proteins and beyond.World journal of microbiology & biotechnology · 2018Review
- Stepwise modifications of genetic parts reinforce the secretory production of nattokinase in Bacillus subtilis.Microbial biotechnology · 2018Article
- Enhanced production of heterologous proteins by Bacillus licheniformis with defective D-alanylation of lipoteichoic acid.World journal of microbiology & biotechnology · 2018Article
- Regulation of the Synthesis and Secretion of the Iron Chelator Cyclodipeptide Pulcherriminic Acid in Bacillus licheniformis.Applied and environmental microbiology · 2018Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSignal peptide peptidases play an important role in the removal of remnant signal peptides in the cell membrane, a critical step for extracellular protein production. Although these proteins are likely a central component for extracellular protein production, there has been a lack of research on whether protein secretion could be enhanced via overexpression of signal peptide peptidases.
resultsIn this study, both nattokinase and α-amylase were employed as prototypical secreted target proteins to evaluate the function of putative signal peptide peptidases (SppA and TepA) in Bacillus licheniformis. We observed dramatic decreases in the concentrations of both target proteins (45 and 49%, respectively) in a sppA deficient strain, while the extracellular protein yields of nattokinase and α-amylase were increased by 30 and 67% respectively in a strain overexpressing SppA. In addition, biomass, specific enzyme activities and the relative gene transcriptional levels were also enhanced due to the overexpression of sppA, while altering the expression levels of tepA had no effect on the concentrations of the secreted target proteins.
conclusionsOur results confirm that SppA, but not TepA, plays an important functional role for protein secretion in B. licheniformis. Our results indicate that the sppA overexpression strain, B. licheniformis BL10GS, could be used as a promising host strain for the industrial production of heterologous secreted proteins.
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