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Many biological processes are mediated by large, complex “protein machines”. The dynamic protein-protein interactions within such complexes are difficult to probe using currently available techniques. Recently, DTR Research Assistant Professor Bo Liu and his colleagues have reported a new “affinity label transfer” technology that begins to address this problem. This technique is the first label transfer technology that does not require covalent modification of the “bait” protein, thus allowing it to be applied to the study of native complexes. The key to the approach is the use of a biarsenical fluorescein (FlAsH) derivative that also contains a biotin tag and a cross-linkable group. FlAsH binds selectively to a six amino acid peptide that can be appended to any protein at the genetic level and thus allow delivery of the cross-linker specifically to that protein. Activation of the cross-linker results in covalent coupling to neighboring proteins. The FlAsH-peptide complex can be dissociated by boiling the products in dithio, resulting in label transfer to the neighboring protein(s), which can then be characterized by a variety of analytical methods. Current efforts are directed towards the application of this novel technique to the characterization of hormone-receptor complexes and the modification of the system for use in living cells.

Article: Liu, B., et al. (2007) J. Amer. Chem. Soc. 129 (41), 12348 -12349.

Abstract

This work has been highlighted by Nature Chemical Biology (vol. 3, 695 (2007) (doi:10.1038/nchembio1107-695) and Nature Methods.