Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
Maria-Armineh Tossounian1, Maria Baczynska1, William Dalton1
1Department of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Antioxidants (Basel, Switzerland)
|July 27, 2022
Summary
Coenzyme A (CoA) protects cells by binding to proteins, forming CoAlated proteins. This study catalogs these proteins and analyzes how CoA stabilizes them, revealing key interactions and binding modes.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Stress Response
Background:
- Coenzyme A (CoA) is crucial for metabolism and gene regulation.
- CoA exhibits antioxidant properties through protein binding (CoAlation) under stress.
Purpose of the Study:
- To compile and analyze known CoAlated proteins and their functions.
- To investigate the structural basis of CoA-protein interactions in CoAlation.
Main Methods:
- Integration of CoAlated protein data into mammalian and bacterial datasets (CoAlomes).
- Utilized anti-CoA antibodies and LC-MS/MS for protein identification.
- Analyzed 35 published CoAlated protein structures.
Main Results:
- Identified 2093 CoAlated proteins with 2862 CoAlation sites.
- CoAlation is prevalent in metabolic, stress response, and protein synthesis pathways.
- Discovered specific interactions stabilizing CoA segments (pantetheine tail, ADP moiety).
Conclusions:
- CoAlation is a widespread post-translational modification with significant biological roles.
- CoA's flexibility allows adaptation to diverse protein microenvironments.
- Proposed three distinct modes of CoA binding to proteins.
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