ArticleFEMS microbiology letters2020
Analysis of disulphide bond linkage between CoA and protein cysteine thiols during sporulation and in spores of Bacillus species.
Article in FEMS microbiology letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Two new factors modulatingmSphere · 2026Article
- Role of Redox-Induced Protein Modifications in Spermatozoa in Health and Disease.Antioxidants (Basel, Switzerland) · 2025Review
- A Unique Mode of Coenzyme A Binding to the Nucleotide Binding Pocket of Human Metastasis Suppressor NME1.International journal of molecular sciences · 2023Article
- Article
- Discovery and functional characterisation of protein CoAlation and the antioxidant function of coenzyme A.BBA advances · 2023Article
- Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions.Antioxidants (Basel, Switzerland) · 2022Article
- Article
- Regulation of metastasis suppressor NME1 by a key metabolic cofactor coenzyme A.Redox biology · 2021Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
Abstract
Spores of Bacillus species have novel properties, which allow them to lie dormant for years and then germinate under favourable conditions. In the current work, the role of a key metabolic integrator, coenzyme A (CoA), in redox regulation of growing cells and during spore formation in Bacillus megaterium and Bacillus subtilis is studied. Exposing these growing cells to oxidising agents or carbon deprivation resulted in extensive covalent protein modification by CoA (termed protein CoAlation), through disulphide bond formation between the CoA thiol group and a protein cysteine. Significant protein CoAlation was observed during sporulation of B. megaterium, and increased largely in parallel with loss of metabolism in spores. Mass spectrometric analysis identified four CoAlated proteins in B. subtilis spores as well as one CoAlated protein in growing B. megaterium cells. All five of these proteins have been identified as moderately abundant in spores. Based on these findings and published studies, protein CoAlation might be involved in facilitating establishment of spores' metabolic dormancy, and/or protecting sensitive sulfhydryl groups of spore enzymes.
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