Browse by author
Lookup NU author(s): Isa Gokce, Professor Jeremy LakeyORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
The third domain of the periplasmic protein TolA from Escherichia coli (TolAIII) was used as a fusion partner in the expression of various proteins from bacteria and eukaryotes. TolAIII is small domain, expressed in high yields as a soluble protein in the cytoplasm of E. coli. Proteins were linked to the C-terminus of TolAIII by a short flexible linker containing sites for endopeptidases. Three different vectors were prepared, containing sites for enterokinase, thrombin or factor Xa. Fusion proteins also contain a His6-Ser2 tag at their N-terminus for easier purification. Up to 90 mg fusion protein per liter bacterial culture was obtained using these vectors. Colicin N R-domain was expressed with this system as a fusion and processed further for functional studies. The yield of final pure R-domain was doubled as compared to the direct expression. The system may prove to be useful in the preparation of other peptides and proteins. © 2002 Elsevier Science (USA). All rights reserved.
Author(s): Anderluh G, Gokce I, Lakey JH
Publication type: Article
Publication status: Published
Journal: Protein Expression and Purification
Year: 2003
Volume: 28
Issue: 1
Pages: 173-181
ISSN (print): 1046-5928
ISSN (electronic): 1096-0279
Publisher: Academic Press
URL: http://dx.doi.org/10.1016/S1046-5928(02)00681-2
DOI: 10.1016/S1046-5928(02)00681-2
PubMed id: 12651122
Altmetrics provided by Altmetric