Optimization of a Bacillus sp signal peptide for improved recombinant protein secretion and cell viability in Escherichia coli: Is there an optimal signal peptide design?
Recombinant protein fused to an N-terminal signal peptide can be translocated to the periplasm and, eventually, to the extracellular medium of Escherichia coli under specific conditions. In this communication, we described the use and optimization of a heterologous signal peptide (G1 signal peptide) from a Bacillus sp for improved recombinant protein secretion and cell viability in E. coli. Significant advantages in maintaining high cell viability and high specificity of target protein secretion were achieved by using G1 signal peptide compared to the well-known PelB signal peptide. Signal peptide sequence analysis and site-directed mutagenesis of G1 signal peptide demonstrated that an 'MKK' sequence in n-region and the presence of a helix-breaking residue at the centre of h-region are important elements for the design of an optimal signal peptide.
Department of Bioprocess Engineering, Universiti Teknologi Malaysia, Skudai, Johor Malaysia.
Kheng Oon
KO
Low
Mohd Anuar
MA
Jonet
Noor Faizah
NF
Ismail
Rosli Md
RM
Illias
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D050296:Microbial Viability; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019897:Periplasm / Q000378:metabolism; D021382:Protein Sorting Signals / Q000235:genetics*; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D012107:Research Design
D021382:Protein Sorting Signals; D011994:Recombinant Proteins