Export incompatibility of N-terminal basic residues in a mature polypeptide of Eschericbia coli can be alleviated by optimising the signal peptide

1990 ◽  
Vol 221 (3) ◽  
pp. 466-474 ◽  
Author(s):  
Sheila Maclntyre ◽  
Marie-Luise Eschbach ◽  
Bettina Mutschler
Keyword(s):  
Signal Peptide ◽  
Mature Polypeptide

scholarly journals Characterization of lysosomal acid lipase mutations in the signal peptide and mature polypeptide region causing Wolman disease

2001 ◽  
Vol 42 (7) ◽  
pp. 1033-1040 ◽  
Author(s):  
Oliver Zschenker ◽  
Nikola Jung ◽  
Julia Rethmeier ◽  
Sabine Trautwein ◽  
Stefanie Hertel ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Acid Lipase ◽  
Wolman Disease ◽  
Lysosomal Acid ◽  
Lysosomal Acid Lipase ◽  
Mature Polypeptide

A Bacterial Signal Peptide Increases Mucociliary Clearance in Explanted Mouse Trachea

Pneumologie ◽  
2016 ◽  
Vol 70 (07) ◽  
Author(s):  
W Kummer ◽  
A Perniß ◽  
B Bufe ◽  
G Krasteva-Christ
Keyword(s):  
Signal Peptide ◽  
Mucociliary Clearance

Enhancing Expression and Accumulation of Foreign Proteins by Using the Signal Peptide of GlutelinGluA-2in Endosperm of Transgenic Rice

2015 ◽  
Vol 41 (4) ◽  
pp. 524
Author(s):  
Hong-Mei WANG ◽  
Chang-Quan ZHANG ◽  
Qian-Feng LI ◽  
Samuel Sing-Min SUN ◽  
Qiao-Quan LIU ◽  
...  
Keyword(s):  
Transgenic Rice ◽  
Signal Peptide ◽  
Foreign Proteins

Suitable Signal Peptides for Secretory Production of Recombinant Granulocyte Colony Stimulating Factor in Escherichia coli

2020 ◽  
Vol 14 (4) ◽  
pp. 269-282
Author(s):  
Sadra S. Tehrani ◽  
Golnaz Goodarzi ◽  
Mohsen Naghizadeh ◽  
Seyyed H. Khatami ◽  
Ahmad Movahedpour ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Signal Peptide ◽  
Fusion Proteins ◽  
Inclusion Bodies ◽  
Clinical Aspects ◽  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
E Coli ◽  
Secretory Production ◽  
Stimulating Factor

Background: Granulocyte colony-stimulating factor (G-CSF) expressed in engineered Escherichia coli (E. coli) as a recombinant protein is utilized as an adjunct to chemotherapy for improving neutropenia. Recombinant proteins overexpression may lead to the creation of inclusion bodies whose recovery is a tedious and costly process. To overcome the problem of inclusion bodies, secretory production might be used. To achieve a mature secretory protein product, suitable signal peptide (SP) selection is a vital step. Objective: In the present study, we aimed at in silico evaluation of proper SPs for secretory production of recombinant G-CSF in E. coli. Methods: Signal peptide website and UniProt were used to collect the SPs and G-CSF sequences. Then, SignalP were utilized in order to predict the SPs and location of their cleavage site. Physicochemical features and solubility were investigated by ProtParam and Protein-sol tools. Fusion proteins sub-cellular localization was predicted by ProtCompB. Results: LPP, ELBP, TSH, HST3, ELBH, AIDA and PET were excluded according to SignalP. The highest aliphatic index belonged to OMPC, TORT and THIB and PPA. Also, the highest GRAVY belonged to OMPC, ELAP, TORT, BLAT, THIB, and PSPE. Furthermore, G-CSF fused with all SPs were predicted as soluble fusion proteins except three SPs. Finally, we found OMPT, OMPF, PHOE, LAMB, SAT, and OMPP can translocate G-CSF into extracellular space. Conclusion: Six SPs were suitable for translocating G-CSF into the extracellular media. Although growing data indicate that the bioinformatics approaches can improve the precision and accuracy of studies, further experimental investigations and recent patents explaining several inventions associated to the clinical aspects of SPs for secretory production of recombinant GCSF in E. coli are required for final validation.

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