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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
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Dataset of wheat HSP90.2 chaperome
Yue-Ting Guo1, Yan Yan1, Guo-Liang Zhang1
1School of Life Sciences, Fudan University, Shanghai 200438, China.
Data in Brief
|July 18, 2024
Summary
This study identified over 1500 wheat Heat Shock Protein 90.2 (HSP90.2) clients, revealing their cellular locations and functions. This provides insights into post-translational regulation in wheat.
Area of Science:
- Plant molecular biology
- Proteomics
- Biochemistry
Background:
- Wheat (Triticum aestivum L.) is a vital global staple crop.
- Heat Shock Protein 90 (HSP90) is a crucial chaperone protein involved in cellular processes like protein folding.
- HSP90.2 plays a significant role in wheat cellular functions.
Purpose of the Study:
- To identify and characterize HSP90.2 client proteins in wheat.
- To understand the distribution and functions of these clients within the cell.
- To explore the role of HSP90.2 in plant responses, such as to stripe rust.
Main Methods:
- Proteomic analysis of wheat (Triticum aestivum L.) whole genome.
- Identification of HSP90.2 clients using C terminus and full-length protein detection.
- Bioinformatic analysis to determine client localization and functions.
Main Results:
- Over 1500 HSP90.2 client proteins were identified in wheat.
- The majority of clients (over 60%) are located in the cytosol, nucleus, and chloroplasts.
- Specific client groups were enriched in different HSP90.2 domains, including cytoskeleton, ethylene biosynthesis, and hypersensitive response pathways.
Conclusions:
- The wheat HSP90.2 chaperome is extensive, encompassing over 1500 proteins.
- HSP90.2 clients are distributed across key cellular compartments and involved in diverse biological processes.
- This dataset enables the study of proteins regulated by HSP90.2 at the post-translational level, offering insights into wheat stress responses.
