© WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
December 19, 2016
Very Important Paper: A Bifunctional Amino Acid Enables Both Covalent Chemical Capture and Isolation of in Vivo Protein--Protein Interactions
Cassandra M. Joiner+, Meghan E. Breen+, James Clayton, and Anna K. Mapp*
In vivo covalent chemical capture by using photo-activatable unnatural amino acids is a powerful tool for the identification of transient protein--protein interactions (PPIs) in their native environment, however, the isolation and characterization of the crosslinked complexes can be challenging. Now, A.K. Mapp (University of Michigan, U.S.A.) and co-workers report a strategy using the bifunctional unnatural amino acid, BPKyne, to capture and directly label transient PPIs in their native environment. Functionalization after crosslinking with a biotin--azide probe enabled the isolation of transcriptional protein complexes from yeast cells. BPKyne expands the toolbox for the discovery of novel PPIs in live cells and can be extended to other biological systems.
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