In vivo phosphorylation of a peptide tag for protein purification
Biotechnology Letters, ISSN: 1573-6776, Vol: 38, Issue: 5, Page: 767-772
2016
- 4Citations
- 16Captures
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Article Description
Objectives: To design a new system for the in vivo phosphorylation of proteins in Escherichia coli using the co-expression of the α-subunit of casein kinase II (CKIIα) and a target protein, (Nanofitin) fused with a phosphorylatable tag. Results: The level of the co-expressed CKIIα was controlled by the arabinose promoter and optimal phosphorylation was obtained with 2 % (w/v) arabinose as inductor. The effectiveness of the phosphorylation system was demonstrated by electrophoretic mobility shift assay (NUT-PAGE) and staining with a specific phosphoprotein-staining gel. The resulting phosphorylated tag was also used to purify the phosphoprotein by immobilized metal affinity chromatography, which relies on the specific interaction of phosphate moieties with Fe(III). Conclusion: The use of a single tag for both the purification and protein array anchoring provides a simple and straightforward system for protein analysis.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84954349940&origin=inward; http://dx.doi.org/10.1007/s10529-016-2040-4; http://www.ncbi.nlm.nih.gov/pubmed/26758722; http://link.springer.com/10.1007/s10529-016-2040-4; https://dx.doi.org/10.1007/s10529-016-2040-4; https://link.springer.com/article/10.1007/s10529-016-2040-4
Springer Science and Business Media LLC
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