Analysis of disulphide bond linkage between CoA and protein cysteine thiols during sporulation and in spores of Bacillus species.
Bacillus species
bacterial spores
coenzyme A
oxidative stress
protein CoAlation
sporulation
Journal
FEMS microbiology letters
ISSN: 1574-6968
Titre abrégé: FEMS Microbiol Lett
Pays: England
ID NLM: 7705721
Informations de publication
Date de publication:
22 12 2020
22 12 2020
Historique:
received:
02
06
2020
accepted:
24
10
2020
pubmed:
19
11
2020
medline:
6
8
2021
entrez:
18
11
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33206970
pii: 5989695
doi: 10.1093/femsle/fnaa174
pmc: PMC8127865
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Disulfides
0
Sulfhydryl Compounds
0
Cysteine
K848JZ4886
Coenzyme A
SAA04E81UX
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Medical Research Council
ID : MC_U105184326
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/P028225/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L010410/1
Pays : United Kingdom
Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of FEMS.
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