Engineered Aryl Azide Ligase for Site-Specific Mapping of Protein-Protein Interactions through Photo-Cross-Linking

Engineered Aryl Azide Ligase for Site-Specific Mapping of Protein-Protein Interactions through Photo-Cross-Linking

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 r...

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Veröffentlicht in:Angewandte Chemie (International ed.) 2008-09, Vol.47 (37), p.7018-7021
Hauptverfasser: Baruah, Hemanta, Puthenveetil, Sujiet, Choi, Yoon-Aa, Shah, Samit, Ting, Alice Y
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine Triphosphate - chemistry
Azides - chemistry
Binding Sites
Cell Line
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
HeLa Cells
Humans
ligases
Ligases - chemistry
Ligases - genetics
Molecular Probes - chemistry
Mutation
Peptides - chemistry
photo-cross-linking
Photochemistry
Protein Engineering
Protein Interaction Mapping - methods
protein interactions
site-specific labeling
Thioctic Acid - chemistry
Ultraviolet Rays
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Zusammenfassung: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200802088