Related Experiment Video

Updated: Jun 27, 2026

Preparation of Chloroplast Sub-compartments from Arabidopsis for the Analysis of Protein Localization by Immunoblotting or Proteomics
10:28

Preparation of Chloroplast Sub-compartments from Arabidopsis for the Analysis of Protein Localization by Immunoblotting or Proteomics

Published on: October 19, 2018

Arabidopsis HSP90C and SecA1 Have Distinct Client-Binding Modalities to the Thylakoid SEC Client Protein PsbO1

Adheip Monikantan Nair1,2, Leonardo Tullo1,2, Kenneth Andrei Espinosa2

  • 1Department of Cell & Systems Biology, University of Toronto, Toronto, ON M5S 1A1, Canada.

Biomolecules
|June 26, 2026
PubMed
Summary

Heat shock protein 90C (HSP90C) and SecA1 chaperone interactions are crucial for chloroplast protein transport. This study reveals HSP90C binds PsbO1 at multiple sites, influencing SecA1 activity for thylakoid protein transport.

Keywords:
HSP90CSecA1chloroplast proteostasischloroplast stromaprotein translocationthylakoid membrane

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