AI Article Synopsis
- Researchers created a new strategy using light-sensitive probes to control the activity of SENPs, which are enzymes related to SUMO (Small Ubiquitin-like Modifier) proteins.
- The method involves using photocaged glycine to temporarily deactivate SUMO-2 probes, preventing unwanted reactions until activated by light.
- This activated probe can capture SENPs in living cells, allowing for detailed studies of SUMO-related enzymes over time.
Article Abstract
The transiently-activated SUMO probes are conducive to understand the dynamic control of SENPs activity. Here, we developed a photocaged glycine-assisted strategy for the construction of on demand-activated SUMO-ABPs. The light-sensitive groups installed at G and G backbone of SUMO-2 can temporarily block probes activity and hamper aspartimide formation, respectively, which enabled the efficient synthesis of inert SUMO-2 propargylamide (PA). The probe could be activated to capture SENPs upon photo-irradiation not only in vitro but also in intact cells, providing opportunities to further perform intracellular time-resolved proteome-wide profiling of SUMO-related enzymes.
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| http://dx.doi.org/10.1016/j.bmcl.2023.129460 | DOI Listing |
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