Issue 12, 2022

Intracellular photocatalytic-proximity labeling for profiling protein–protein interactions in microenvironments

Abstract

Intracellular photocatalytic-proximity labeling (iPPL) was developed to profile protein–protein interactions in the microenvironment of living cells. Acriflavine was found to be an efficient cell-membrane-permeable photocatalyst for introduction into the genetically HaloTag-fused protein of interest for iPPL with a radical labeling reagent, 1-methyl-4-arylurazole. iPPL was applied to the histone-associated protein H2B in HaloTag-H2B expressing HEK293FT cells. The proteins directly interacting with histones and RNA-binding proteins were selectively labeled in the intracellular environment, suggesting that the iPPL method has a smaller labeling radius (CA. 6 nm) than the BioID and APEX methods.

Graphical abstract: Intracellular photocatalytic-proximity labeling for profiling protein–protein interactions in microenvironments

Supplementary files

Article information

Article type
Communication
Submitted
12 Here 2021
Accepted
05 Gen. 2022
First published
05 Gen. 2022

Chem. Commun., 2022,58, 1926-1929

Intracellular photocatalytic-proximity labeling for profiling protein–protein interactions in microenvironments

M. Tsushima, S. Sato, K. Miura, T. Niwa, H. Taguchi and H. Nakamura, Chem. Commun., 2022, 58, 1926 DOI: 10.1039/D1CC05764B

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