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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?

Low, K. O. and Jonet, M. A. and Ismail, N. F. and Illias, R. M. (2012) 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? Bioengineered Bugs, 3 (6). pp. 334-338. ISSN 1949-1018

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Official URL: http://dx.doi.org/10.4161/bioe.21454

Abstract

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.

Item Type:Article
Uncontrolled Keywords:periplasm, protein secretion, E. coli
Subjects:T Technology > TP Chemical technology
Divisions:Chemical Engineering
ID Code:47317
Deposited By: Narimah Nawil
Deposited On:22 Jun 2015 05:56
Last Modified:31 Mar 2019 08:38

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