An Engineered Aryl Azide Ligase for Site‐Specific Mapping of Protein–Protein Interactions through Photo‐Cross‐Linking
- 27 August 2008
- journal article
- research article
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 47 (37), 7018-7021
- https://doi.org/10.1002/anie.200802088
Abstract
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.Keywords
This publication has 38 references indexed in Scilit:
- Protein−Protein Interaction Detection in Vitro and in Cells by Proximity BiotinylationJournal of the American Chemical Society, 2008
- Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probesNature Biotechnology, 2007
- Copper-free click chemistry for dynamic in vivo imagingProceedings of the National Academy of Sciences, 2007
- Quantification of dynamic protein complexes using Renilla luciferase fragment complementation applied to protein kinase A activities in vivoProceedings of the National Academy of Sciences, 2007
- Genetically encoding unnatural amino acids for cellular and neuronal studiesNature Neuroscience, 2007
- EXPANDING THE GENETIC CODEAnnual Review of Biophysics, 2006
- Crystal Structure of Lipoate-Protein Ligase A from Escherichia coliJournal of Biological Chemistry, 2005
- Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cellsNature Methods, 2005
- Expanding the Diversity of Unnatural Cell‐Surface Sialic AcidsChemBioChem, 2004
- NEW PHOTOLABELING AND CROSSLINKING METHODSAnnual Review of Biochemistry, 1993