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Bioorthogonal Photocatalytic Decaging-Enabled Mitochondrial Proteomics.

Zongyu Huang1, Ziqi Liu1, Xiao Xie1

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|October 28, 2021
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Summary

We developed CAT-Prox, a novel photocatalytic method for spatiotemporally resolved mitochondrial proteome profiling in living cells. This technique enables precise mapping of mitochondrial proteins, advancing cellular function studies.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Chemical Biology

Background:

  • Understanding subcellular proteomes is vital for cellular function and disease research.
  • Existing proximity labeling methods often lack spatiotemporal control or require genetic manipulation.
  • Mitochondrial proteome analysis is challenging, especially in difficult-to-transfect cells.

Purpose of the Study:

  • To develop a bioorthogonal, photocatalytic proximity labeling strategy for spatiotemporally resolved mitochondrial proteome profiling in living cells.
  • To identify an effective mitochondria-targeting photocatalyst for controlled protein labeling.
  • To demonstrate the utility of the method in various cell types and under stimulation conditions.

Main Methods:

  • Developed a photocatalytic decaging-enabled proximity labeling strategy (CAT-Prox).
  • Identified and validated Ir(ppy)2bpy as a bioorthogonal, mitochondria-targeting photocatalyst.
  • Utilized photocontrolled release of a reactive Michael acceptor for proximity labeling in mitochondria.
  • Applied CAT-Prox to proteome profiling in HeLa and RAW264.7 cells, including dynamic analysis upon LPS stimulation.

Main Results:

  • CAT-Prox enabled spatiotemporally resolved mitochondrial proteome profiling in live cells.
  • Achieved high mitochondria specificity (~70%) for up to 300 enriched proteins.
  • Successfully profiled mitochondrial proteomes in both HeLa and macrophage RAW264.7 cells.
  • Demonstrated dynamic changes in mitochondrial proteome upon lipopolysaccharide stimulation.

Conclusions:

  • CAT-Prox provides a general, catalytic, and nongenetic alternative to enzyme-based proximity labeling.
  • The method offers precise spatiotemporal control for dissecting subcellular proteomes in diverse live cell settings.
  • Facilitates advanced studies of mitochondrial function and dynamics in health and disease.