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Issue 4, 2016
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‘Traceless’ tracing of proteins – high-affinity trans-splicing directed by a minimal interaction pair

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Abstract

Protein trans-splicing mediated by split inteins is a powerful technique for site-specific protein modification. Despite recent developments there is still an urgent need for ultra-small high-affinity intein tags for in vitro and in vivo approaches. To date, only very few in-cell applications of protein trans-splicing have been reported, all limited to C-terminal protein modifications. Here, we developed a strategy for covalent N-terminal intein-mediated protein labeling at (sub) nanomolar probe concentrations. Combined with a minimal synthetic lock-and-key element, the affinity between the intein fragments was increased more than 50-fold to 10 nM. Site-specific and efficient ‘traceless’ protein modification by high-affinity trans-splicing is demonstrated at nanomolar concentrations in living mammalian cells.

Graphical abstract: ‘Traceless’ tracing of proteins – high-affinity trans-splicing directed by a minimal interaction pair

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Supplementary files

Article information


Submitted
09 Aug 2015
Accepted
18 Dec 2015
First published
21 Dec 2015

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2016,7, 2646-2652
Article type
Edge Article
Author version available

‘Traceless’ tracing of proteins – high-affinity trans-splicing directed by a minimal interaction pair

M. Braner, A. Kollmannsperger, R. Wieneke and R. Tampé, Chem. Sci., 2016, 7, 2646
DOI: 10.1039/C5SC02936H

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