ReviewMicrobial cell factories2018
Signal peptides for recombinant protein secretion in bacterial expression systems.
Review in Microbial cell factories, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.
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Who cites it
130 citing papers in PubMed.
- Enhanced biodegradation of bisphenol S by laccase encapsulated in copper-nucleotide metal-organic frameworks.World journal of microbiology & biotechnology · 2026Article
- Multi-parameter optimization of recombinant protein secretion in Bacillus subtilis: a review.Microbial cell factories · 2026Review
- Functional mapping and engineering of the Sec translocon unlocked by a cell-free system.Science advances · 2026Article
- Signal peptide engineering of a novel M4 family keratinase and the action mechanism in promoting pepper tolerance to salt stress through KerJY23-hydrolyzed feather waste.Synthetic and systems biotechnology · 2026Article
- High-cell-density Escherichia coli-based nanobody production: benchmarking of subcellular targeting, strain background and process development strategies.Microbial cell factories · 2026Article
- Advances in Key Genetic Elements and Strategies for High-Yield Heterologous Protein Expression inJournal of fungi (Basel, Switzerland) · 2026Review
- Exploration of Length and Hydrophobicity Requirements for Optimal α-Amylase Secretion in Bacillus subtilis Based on Rational Design.Microbial biotechnology · 2026Article
- A signal peptide-guided approach towards in situ functionalization of bacterial nanocellulose in Komagataeibacter rhaeticus.Journal of biological engineering · 2026Article
- How far can you go? Extrapolating values of catalytic activity from known protein landscapes in natural and directed evolution.Chemical Society reviews · 2026Review
- A standardized toolkit for programmable protein secretion and surface display inbioRxiv : the preprint server for biology · 2026Article
- Advances, challenges, and future directions towards a cellulolytic Escherichia coli.Biotechnology for biofuels and bioproducts · 2026Review
- Development and application of a genotyping by target sequencing single-nucleotide polymorphism array panel in Salix suchowensis.BMC genomics · 2026Article
- Engineered Escherichia coli as a microbial cell factory for intracellular protein delivery: strains, vectors, mechanisms, and therapeutic applications.Microbial cell factories · 2026Review
- Senotoxins target senescence via lipid binding specificity, ion imbalance and lipidome remodeling.Nature aging · 2026Article
- High-Throughput Screening of Co-Protoporphyrin IX-Binding Proteins for Enhanced Hydrogen Production.Molecules (Basel, Switzerland) · 2026Article
- Recombinant Expression and Antimicrobial Mechanism of Cysteine-Rich Antimicrobial Peptides fromMarine drugs · 2026Article
- Rapid Identification of Superior Endogenous Signal Peptides for Heterologous Protein Secretion by Corynebacterium glutamicum Through Modular Cloning and Automation.Microbial biotechnology · 2026Article
- Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026Article
- Article
- The transcriptomic response of Staphylococcus equorum KS1030 to Lincomycin stress reveals transporters associated with horizontal gene transfer.Scientific reports · 2025Article
70 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
The secretion of biotechnologically or pharmaceutically relevant recombinant proteins into the culture supernatant of a bacterial expression host greatly facilitates their downstream processing and significantly reduces the production costs. The first step during the secretion of a desired target protein into the growth medium is its transport across the cytoplasmic membrane. In bacteria, two major export pathways, the general secretion or Sec pathway and the twin-arginine translocation or Tat pathway, exist for the transport of proteins across the plasma membrane. The routing into one of these alternative protein export systems requires the fusion of a Sec- or Tat-specific signal peptide to the amino-terminal end of the desired target protein. Since signal peptides, besides being required for the targeting to and membrane translocation by the respective protein translocases, also have additional influences on the biosynthesis, the folding kinetics, and the stability of the respective target proteins, it is not possible so far to predict in advance which signal peptide will perform best in the context of a given target protein and a given bacterial expression host. As outlined in this review, the most promising way to find the optimal signal peptide for a desired protein is to screen the largest possible diversity of signal peptides, either generated by signal peptide variation using large signal peptide libraries or, alternatively, by optimization of a given signal peptide using site-directed or random mutagenesis strategies.
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