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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
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Thiol-Redox Proteomics to Study Reversible Protein Thiol Oxidations in Bacteria
Martina Rossius1, Falko Hochgräfe2, Haike Antelmann3
1Institute for Biology-Microbiology, Freie Universität Berlin, Berlin, Germany.
Methods in Molecular Biology (Clifton, N.J.)
|September 28, 2018
Summary
This study details two thiol-redox proteomics methods for detecting protein S-thiolations in Gram-positive bacteria. These techniques identify proteins undergoing reversible thiol oxidation during normal growth and oxidative stress.
Area of Science:
- Redox biology
- Proteomics
- Microbiology
Background:
- Thiol-redox proteomics is crucial for understanding cellular redox states.
- Reversible protein thiol oxidation occurs under normal and stress conditions.
- Current methods involve complex alkylation and reduction steps.
Purpose of the Study:
- To describe two thiol-redox proteomics methods for detecting protein S-thiolations.
- To apply these methods in Gram-positive bacteria.
- To leverage previously successful techniques.
Main Methods:
- Direct shotgun proteomics approach.
- Fluorescent-label thiol-redox proteomics method.
- Differential alkylation of thiols following disulfide bond reduction.
Main Results:
- Successful application of two distinct thiol-redox proteomics methods.
- Detection of protein S-thiolations in Gram-positive bacteria.
- Demonstration of method utility in prior research.
Conclusions:
- The described methods are effective for analyzing protein thiol modifications in bacteria.
- These techniques contribute to the advancement of redox biology research.
- The methods provide insights into cellular responses to oxidative stress.
Keywords:
Fluorescent-based redox proteomicsMass spectrometryProtein S-thiolationsReversible thiol oxidationsThiol trappingMore Related Videos
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