<Emphasis Type="Italic">In vivo</Emphasis>site-specific biotinylation of proteins within the secretory pathway using a single vector system |
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Authors: | Andrea Predonzani Francesca Arnoldi Alejandro López-Requena Oscar R Burrone |
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Institution: | (1) Molecular Immunology Group, International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34012 Trieste, Italy;(2) Department of Antibody Engineering, Center of Molecular Immunology, P.O. Box 16040, Havana, 11600, Cuba |
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Abstract: | Background Due to its extremely high strength, the interaction between biotin and (strept)avidin has been exploited for a large number
of biotechnological applications. Site-specific biotinylation of proteins in vivo can be achieved by co-expressing in mammalian cells the protein of interest fused to a 15 amino acid long Biotin Acceptor
Peptide (BAP) and the bacterial biotin-protein ligase BirA, which specifically recognizes and attaches a biotin to the single
lysine residue of the BAP sequence. However, this system is mainly based on the contemporaneous use of two different plasmids
or on induction of expression of two proteins through an IRES-driven mechanism. |
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Keywords: | |
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