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Biogenesis, quality control and structural dynamics of proteins as explored in living cells via site-directed photo-crosslinking.

Protein Science 2019 April 20
Protein biogenesis and quality control are essential for maintaining a functional pool of proteins and involve numerous protein factors that dynamically and transiently interact with each other and with the substrate proteins in living cells. Conventional methods are hardly effective for studying such dynamic, transient, and weak protein-protein interactions as occur in cells. Herein we review how the site-directed photo-crosslinking approach, which relies on the genetic incorporation of a photo-reactive unnatural amino acid into a protein of interest at selected individual amino acid residue position and the covalent trapping of the interacting proteins upon ultraviolent (UV) irradiation, has become a highly efficient way to explore these aspects of protein contacts in living cells. For example, in the past decade, this approach has allowed the profiling of the in vivo substrate proteins of chaperones or proteases under both physiologically optimal or stressful (e.g., acidic) conditions, mapping residues located at protein interfaces, identifying new protein factors involved in the biogenesis of membrane proteins, trapping transiently formed protein complexes, as well as snapshotting different structural states of a protein. We anticipate that the site-directed photo-crosslinking approach will play a fundamental role in dissecting the detailed mechanisms of protein biogenesis, quality control and dynamics in the future. This article is protected by copyright. All rights reserved.

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