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Author Spotlight: Combining Proximity Ligand Assay with Gamma-H2AX Staining to Characterize Protein Interactions in DNA Damage Response
Published on: August 2, 2024
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The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage
Andrew W Truman1, Kolbrun Kristjansdottir2, Donald Wolfgeher1
1Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.
Data in Brief
|July 29, 2015
Summary
Molecular chaperones Hsp70 and Hsp90 are crucial for the DNA damage response (DDR). This study identified 256 protein interactors, revealing how these chaperones function in cellular repair pathways.
Area of Science:
- Molecular Biology
- Cellular Biology
- Proteomics
Background:
- Molecular chaperones, including Hsp70 and Hsp90, play vital roles in cellular processes.
- These chaperones are known to be involved in the cellular response to DNA damage.
Purpose of the Study:
- To investigate the protein network of Hsp70 and Hsp90 in the DNA damage response (DDR).
- To characterize the interactomes of yeast Hsp70 (Ssa1) and Hsp90 (Hsp82) under normal and DNA-damaging conditions.
Main Methods:
- Quantitative affinity-purification mass spectrometry (AP-MS) proteomics.
- Analysis of protein-chaperone interactions in yeast before and after methyl methanesulfonate exposure.
Main Results:
- Identified 256 chaperone interactors, with 146 being novel.
- Observed that most chaperone interactions remained constant under DNA damage.
- Found 5 specific proteins (Coq5, Ast1, Cys3, Ydr210c, Rnr4) showed increased interaction with Ssa1 and/or Hsp82 upon DNA damage.
Conclusions:
- The study elucidates the protein interaction network of Hsp70 and Hsp90 in the DDR.
- Specific proteins dynamically alter their interaction with chaperones in response to DNA damage, suggesting a role in the repair mechanism.
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