Related Experiment Video
Updated: May 20, 2026

Generation of Fluorescent Protein Fusions in Candida Species
Published on: March 4, 2017
Preparation of unnatural N-to-N and C-to-C protein fusions
Martin D Witte1, Juan J Cragnolini, Stephanie K Dougan
1Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Abstract:
Standard genetic approaches allow the production of protein composites by fusion of polypeptides in head-to-tail fashion. Some applications would benefit from constructions that are genetically impossible, such as the site-specific linkage of proteins via their N or C termini, when a remaining free terminus is required for biological activity. We developed a method for the production of N-to-N and C-to-C dimers, with full retention of the biological activity of both fusion partners and without inflicting chemical damage on the proteins to be joined. We use sortase A to install on the N or C terminus of proteins of interest the requisite modifications to execute a strain-promoted copper-free cycloaddition and show that the ensuing ligation proceeds efficiently. Applied here to protein-protein fusions, the method reported can be extended to connecting proteins with any entity of interest.
Related Concept Videos
Tagging and Fusion Proteins
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
