Transport of heterologous proteins to the periplasmic space of Pseudomonas fluorescens using a variety of native signal sequences.
Bacterial expression of recombinant proteins containing disulfide bonds is facilitated by transport of the proteins to the periplasmic space. Several Pseudomonas fluorescens signal sequences have been identified that efficiently direct proteins to the periplasm and provide solubility and yield advantages over the production of proteins fused to the PelB signal sequence in E. coli. For a single chain antibody fragment, the final yield varied from about 1 g/l to 10 g/l when expression in P. fluorescens involved fusion to various P. fluorescens signal sequences.
Retallack
Diane M
DM
The Dow Chemical Company, Core Biotechnology Research and Development, 5501 Oberlin Dr, San Diego, CA 92121, USA. dmretallack@dow.com
Schneider
J Carrie
JC
Mitchell
Jon
J
Chew
Lawrence
L
Liu
Huizhu
H
D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D005822:Genetic Vectors / Q000235:genetics; D019897:Periplasm / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000235:genetics / Q000502:physiology*; D021381:Protein Transport; D011551:Pseudomonas fluorescens / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D017422:Sequence Analysis, DNA
D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins