This work was supported by the US National Institutes of Health (grant nos.: R01 GM072670 and P20 GM072029), the Sloan Foundation, and the Dreyfus Foundation. Samsung Corporation provided a Lee Kun Hee scholarship to Y.-A.C. We thank Susan M. Lydon for her assistance with graphics. We thank Kathleen T. Xie and Jackie Chan for help with site-directed mutagenesis experiments and Marta Fernández-Suárez for assistance and advice.
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Communication
An Engineered Aryl Azide Ligase for Site-Specific Mapping of Protein–Protein Interactions through Photo-Cross-Linking†
Article first published online: 4 AUG 2008
DOI: 10.1002/anie.200802088
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue
Angewandte Chemie International Edition
Volume 47, Issue 37, pages 7018–7021, September 1, 2008
Additional Information
How to Cite
Baruah, H., Puthenveetil, S., Choi, Y.-A., Shah, S. and Ting, Alice Y. (2008), An Engineered Aryl Azide Ligase for Site-Specific Mapping of Protein–Protein Interactions through Photo-Cross-Linking. Angew. Chem. Int. Ed., 47: 7018–7021. doi: 10.1002/anie.200802088
- †
Publication History
- Issue published online: 27 AUG 2008
- Article first published online: 4 AUG 2008
- Manuscript Received: 3 MAY 2008
Funded by
- US National Institutes of Health. Grant Numbers: R01 GM072670, P20 GM072029
- Sloan Foundation
- Dreyfus Foundation
Keywords:
- ligases;
- photo-cross-linking;
- protein engineering;
- protein interactions;
- site-specific labeling
Labeled and linked: The small-molecule binding site of Escherichia coli lipoic acid ligase was re-engineered to accept a fluorinated aryl azide probe in place of lipoic acid. Labeling with this mutant is highly specific for LAP fusion proteins. In cell lysate, FK506 binding protein was labeled and rapamycin-dependent photo-cross-linking to its interaction partner was demonstrated.