Posted by Robert Pearce on November 18, 2013
Dr. Kim Bonger, working with her colleagues in the Chen and Wandless labs, developed a new method to regulate the stability of specific proteins using non-toxic blue light. Kim previously discovered a short peptide sequence that is very destabilizing when it is fused to the C-terminus of proteins. Kim grafted this peptide “degron” onto the C-terminus of the light-sensitive LOV2 domain. In the resting state, this C-terminus is part of an alpha-helix that associates tightly with the rest of the LOV2 domain and the degron cannot be detected by the cellular quality control machinery. However, upon exposure to blue light, this helix becomes disordered and the degron is revealed. The LOV2 domain is rapidly tagged with ubiquitin and degraded by the proteasome. By fusing Kim’s engineered LOV2 domain to the C-terminus of any protein-of-interest, researchers should be able to control the stability of the protein in their experiments by regulating how much blue light their cells receive.
Bonger KM, Rakhit R, Payumo AY, Chen JK, Wandless TJ. General Method for Regulating Protein Stability with Light. ACS Chem Biol. 2013 Nov 8. PMID:24180414