A comprehensive review of signal peptides: Structure, roles, and applications.

@article{Owji2018ACR,
  title={A comprehensive review of signal peptides: Structure, roles, and applications.},
  author={Hajar Owji and Navid Nezafat and Manica Negahdaripour and Ali Hajiebrahimi and Younes Ghasemi},
  journal={European journal of cell biology},
  year={2018},
  volume={97 6},
  pages={
          422-441
        }
}
SPSED: A Signal Peptide Secretion Efficiency Database
TLDR
SPSED is a valuable resource for recombinant protein production and researches in the mechanism of signal peptide secretion, which remains unclear how the signal peptides influence the secretion efficiency of the recombinant proteins.
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TLDR
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TLDR
The in silico evaluation of several peptides to find the most suitable leader peptides for secretory production of α-amylase in B. subtilis predicted as secretory signal peptides which can excrete protein out of the bacteria.
In Silico Study of Different Signal Peptides to Express Recombinant Glutamate Decarboxylase in the Outer Membrane of Escherichia coli
TLDR
The most suitable SP for the expression of recombinant GAD in the outer membrane of E. coli seemed to be torT with a reasonably high D-score, aliphatic index, and GRAVY, followed by ccmH and then pspE, which might be useful in future experimental research.
In silico analysis of suitable signal peptides for secretion of a recombinant alcohol dehydrogenase with a key role in atorvastatin enzymatic synthesis
TLDR
The six selected SPs in the result section were suitable to design a soluble secretory LKADH that accelerate its scale-up production and might be useful in future experimental researches.
Razor: annotation of signal peptides from toxins
TLDR
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Annotating eukaryotic and toxin-specific signal peptides using Razor
TLDR
It is discovered that many defensive proteins across kingdoms harbour a toxin-like signal peptide; some of these defensive proteins have emerged through convergent evolution, e.g.defensin and defensin-like protein families, and phospholipase families.
Analyzing Signal Peptides for Secretory Production of Recombinant Diagnostic Antigen B8/1 from Echinococcus granulosus: An In silico Approach.
TLDR
Among the 39 candidate signal peptides, ENTC2_STAAU and ENTC1_ STAAU are the best ones which are stable and soluble in connection with AgB8/1 and can secrete target protein through Sec pathway and the signal peptide recommended in this investigation are valuable for rational designing of secretorystable and soluble AgB 8/1.
Design of an improved universal signal peptide based on the α-factor mating secretion signal for enzyme production in yeast
TLDR
The optimisation of the α-factor preproleader to improve recombinant enzyme production in S. cerevisiae is described and a guideline to further drive the heterologous production of a particular enzyme based on combinatorial saturation mutagenesis of positions 86th and 87th of theα OPT leader fused to the target protein is suggested.
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TLDR
The present knowledge of Streptomyces leader sequences and the impact of introduced mutations on transcription, translation and secretion of homologous and heterologous proteins is reviewed.
In Silico Evaluation of Different Signal Peptides for the Secretory Production of Human Growth Hormone in E. coli
Various advantages of protein secretion have prompted scientists to search for secretory production of heterologous proteins. Signal peptides are one of the most important factors for prosperous
Molecular engineering of secretory machinery components for high-level secretion of proteins in Bacillus species
TLDR
Recent progress in secretory expression of recombinant proteins in Bacillus species is summarized and advances in molecular engineering of secretory machinery components, construction of signal sequence libraries and identification of functional signal peptide chains are highlighted.
Flanking signal and mature peptide residues influence signal peptide cleavage
TLDR
It is concluded that the peptide segment recognized by SPase I extends to the start of the mature protein to a limited extent, upon a survey of the amino acid residues surrounding the cleavage processing site.
Signal Peptide-Dependent Protein Transport inBacillus subtilis: a Genome-Based Survey of the Secretome
TLDR
The predictions and comparisons in this review pinpoint important differences as well as similarities between protein transport systems in B. subtilis and other well-studied organisms, such as Escherichia coli and the yeast Saccharomyces cerevisiae, which may serve as a lead for future research and applications.
Non-classical protein secretion in bacteria
TLDR
Predicting of disorder reveals that bacterial secretory proteins are more structurally disordered than their cytoplasmic counterparts, thus allowing for the identification of novel non-classically secreted proteins.
Optimisation of signal peptide for recombinant protein secretion in bacterial hosts
TLDR
Several important characteristics and requirements are summarised for the design of a more efficient signal peptide for the production of recombinant proteins in E. coli.
Post‑Targeting Functions of Signal Peptides
TLDR
Examples of post‑targeting functions of membrane‑integral signal peptides, of sign peptides released from the membrane into either the cytosol or endoplasmic reticulum lumen and of signal peptide fragments generated by intramembrane cleavage are described.
How many signal peptides are there in bacteria?
Over the last 5 years proteogenomics (using mass spectroscopy to identify proteins predicted from genomic sequences) has emerged as a promising approach to the high-throughput identification of
Signal peptidase I: Cleaving the way to mature proteins
TLDR
Advances in understanding of how the preprotein interfaces with SPase I during the final stages of translocation will facilitate future development of inhibitors that display a high efficacy againstSPase I function.
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