Optimization of a Heterologous Signal Peptide by Site-Directed Mutagenesis for Improved Secretion of Recombinant Proteins in Escherichia coli-Reference-Cited by-同舟云学术

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Optimization of a Heterologous Signal Peptide by Site-Directed Mutagenesis for Improved Secretion of Recombinant Proteins in Escherichia coli

Published:2012 Issue:1 Volume:22 Page:48-58
ISSN:1660-2412
Container-title:Journal of Molecular Microbiology and Biotechnology
language:en
Short-container-title:J Mol Microbiol Biotechnol

Author:

Jonet Mohd Anuar,Mahadi Nor Muhammad,Murad Abdul Munir Abdul,Rabu Amir,Bakar Farah Diba Abu,Rahim Raha Abdul,Low Kheng Oon,Illias Rosli Md.

Publisher

S. Karger AG

Subject

Molecular Biology,Applied Microbiology and Biotechnology,Microbiology,Biotechnology

Reference36 articles.

1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

2. Recombinant protein expression in Escherichia coli

3. Recombinant protein folding and misfolding in Escherichia coli

4. Glycine Residues in the Hydrophobic Core of the GspB Signal Sequence Route Export toward the Accessory Sec Pathway

5. Improvement of extracellular production of a thermophilic subtilase expressed in Escherichia coli by random mutagenesis of its N-terminal propeptide

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