Dataset Information

Time-Resolved Analysis of Protein-Protein Ensembles using a Destabilizing Domain (TRAPPED) to resolve dynamic interactions of SARS-CoV-2 nsp15

ABSTRACT: Cellular protein-protein interactions are dynamic and can change over time. Current interactomics methods capture steady-state information but lack the ability to differentiate when the interactions occur. This study developed a post-translational method for synchronizing protein accumulation that allows for monitoring of protein-protein interactions of the same protein population over time. The protein of interest is tagged with a destabilizing protein domain, which can be stabilized and labeled by a functionalized small molecule. This system, Time-Resolved Analysis of Protein-Protein Ensembles using a Destabilizing Domain (TRAPPED), was utilized to characterize the interactions of SARS-CoV-2 and SARS-CoV non-structural protein 15 to reveal the timing of key interactions with RNA-binding proteins. TRAPPED can be expanded to study the timing of interactions in other systems including viral infection, secretion pathways, and signal transduction.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Kidney Cell

DISEASE(S): Disease Free

SUBMITTER: Crissey Cameron

LAB HEAD: Lars Plate

PROVIDER: PXD063935 | Pride | 2025-09-29

REPOSITORIES: Pride

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			Action	DRS
	01-018-019-RMJ-20230221-S1nsp15-TMT16-0C_1.raw	Raw
	01-018-019-RMJ-20230221-S1nsp15-TMT16-100C_7.raw	Raw
	01-018-019-RMJ-20230221-S1nsp15-TMT16-10C_2.raw	Raw
	01-018-019-RMJ-20230221-S1nsp15-TMT16-20C_3.raw	Raw
	01-018-019-RMJ-20230221-S1nsp15-TMT16-40C_4.raw	Raw

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Time-Resolved Analysis of Protein-Protein Ensembles Using a Destabilizing Domain to Map Dynamic Interactions of SARS-CoV-2 nsp15.

Cameron Crissey C Clark R Mason RM Metts Adam M AM Jiang Runze M RM Scaggs Toya D TD Kim Kwangho K Sulikowski Gary A GA Plate Lars L

ACS chemical biology 20250901 9

Dynamic protein-protein interactions are key drivers of many cellular processes. Determining the relative sequence and precise timing of these interactions is crucial for elucidating the functional dynamics of biological processes. Here, we developed a time-resolved analysis of protein-protein ensembles using a destabilizing domain (TRAPPED) to study protein-protein interactions in a temporal manner. We have taken advantage of a dihydrofolate reductase-destabilizing domain (DHFR(DD)) that can be ...[more]

PMID: 40889207

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