Abstract
Protein trans-splicing is a posttranslational modification that joins two protein fragments together via a peptide a bond in a process that does not require exogenous cofactors. Towards achieving cellular control, synthetically engineered systems have used a variety of stimuli such as small molecules and light. Recently, split inteins have been engineered to be photoactive by the LOV2 domain (named LOVInC). Herein, we discuss (1) designing of LOV2-activated target proteins (e.g., inteins), (2) selecting feasible splice sites for the extein, and (3) imaging cells that express LOVInC-based target exteins.
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Acknowledgments
This work was funded by grants from the Canadian Cancer Society Research Institute (#701936) and NSERC (#05322-14).
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Qudrat, A., Mosabbir, A., Truong, K. (2017). LOV2-Controlled Photoactivation of Protein Trans-Splicing. In: Mootz, H. (eds) Split Inteins. Methods in Molecular Biology, vol 1495. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6451-2_15
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DOI: https://doi.org/10.1007/978-1-4939-6451-2_15
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