A photo-oxidation driven proximity labeling strategy enables profiling of mitochondrial proteome dynamics in living cells.

ABSTRACT: Mapping the proteomic landscape of mitochondria with spatiotemporal precision plays a pivotal role in elucidating the delicate biological functions and complex relationship with other organelles in a variety of dynamic physiological processes which necessitates efficient and controllable chemical tools. We herein report a photo-oxidation driven proximity labeling strategy to profile the mitochondrial proteome by light dependence in living cells with high spatiotemporal resolution. Taking advantage of organelle-localizable organic photoactivated probes generating reactive species and nucleophilic substrates for proximal protein oxidation and trapping, mitochondrial proteins were selectively labeled by spatially limited reactions in their native environment. Integration of photo-oxidation dr

SUBMITTER: Wang H 

PROVIDER: S-EPMC9580500 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature