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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.

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|September 11, 2023
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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.

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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.