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