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Effects of signal peptide primary structure on efficiency of recombinant Staphylococcus aureus pro-enterotoxin A transmembrane translocation in E. coli cells

Effects of signal peptide primary structure on efficiency of recombinant Staphylococcus aureus... Enterotoxin A containing various leader sequences have been obtained by site-driven mutagenesis. Some of them were capable of providing the translocation of recombinant SEA to E. coli periplasmic space. Structure of C-region of the signal peptide is essential for intracellular protein location. Substitution of a more common to E. coli proproteins Ala-Ser-Ala for the authentic sequence of Val-Asn-Gly is the most important in recognition by signal peptidase type I. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Effects of signal peptide primary structure on efficiency of recombinant Staphylococcus aureus pro-enterotoxin A transmembrane translocation in E. coli cells

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References (15)

Publisher
Springer Journals
Copyright
Copyright © 2010 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Medical Microbiology ; Microbiology ; Biochemistry, general
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683810090036
Publisher site
See Article on Publisher Site

Abstract

Enterotoxin A containing various leader sequences have been obtained by site-driven mutagenesis. Some of them were capable of providing the translocation of recombinant SEA to E. coli periplasmic space. Structure of C-region of the signal peptide is essential for intracellular protein location. Substitution of a more common to E. coli proproteins Ala-Ser-Ala for the authentic sequence of Val-Asn-Gly is the most important in recognition by signal peptidase type I.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Nov 12, 2010

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