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Updated: Jul 16, 2025
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Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
Published on: October 7, 2021
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AP profiling resolves co-translational folding pathway and chaperone interactions in vivo.
Xiuqi Chen1,2,3, Christian M Kaiser2,4
1CMDB Graduate Program, Johns Hopkins University, Baltimore, MD, United States.
Biorxiv : the Preprint Server for Biology
|September 11, 2023
Summary
We developed Arrest Peptide profiling (AP profiling) to measure protein folding during synthesis in live cells. This method reveals how protein structure and chaperones influence co-translational folding pathways.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Protein folding is crucial for cellular function, but co-translational folding remains poorly understood.
- Existing methods struggle to accurately measure folding within the complex cellular environment.
Purpose of the Study:
- To develop a high-throughput method for quantifying co-translational folding in live cells.
- To investigate how protein topology and molecular chaperones influence folding pathways.
Main Methods:
- Developed Arrest Peptide profiling (AP profiling), a novel high-throughput technique.
- Applied AP profiling to study GTPase domains and the impact of chaperone ablation.
Main Results:
- Delineated co-translational folding pathways for GTPase domains, highlighting the role of topology.
- Observed localized folding changes upon chaperone genetic ablation, suggesting functional redundancy mechanisms.
Conclusions:
- AP profiling offers unprecedented resolution and throughput for studying nascent protein folding.
- This work provides insights into cellular folding mechanisms and chaperone interactions.
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