Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 5, Pages 1306-1310Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201307969
Keywords
autocatalysis; chemoenzymatic synthesis; combinatorial mutagenesis; protein engineering; protein semisynthesis
Categories
Funding
- Deutsche Forschungsgemeinschaft [MO1073/3-2, MO1073/5-1]
- Cells-in-Motion excellence cluster [EXC1003]
- German National Merit Foundation
Ask authors/readers for more resources
Protein trans-splicing catalyzed by split inteins is a powerful technique for assembling a polypeptide backbone from two separate parts. However, split inteins with robust efficiencies and short fragments suitable for peptide synthesis are rare and have mostly been artificially created. The novel split intein AceL-TerL was identified from metagenomic data and characterized. It represents the first naturally occurring, atypically split intein. The N-terminal fragment of only 25 amino acids is the shortest natural intein fragment to date and was easily amenable to chemical synthesis with a fluorescent label. Optimal protein trans-splicing activity was observed at low temperatures. Further improved mutants were selected by directed protein evolution. The engineered intein variants with up to 50-fold increased rates showed unprecedented efficiency in chemically labeling of a diverse set of proteins. These inteins should prove valuable tools for protein semi-synthesis and other intein-related biotechnological applications.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available