Functional connexion of bacterioferritin in antibiotic production and morphological differentiation in Streptomyces coelicolor.
Streptomyces coelicolor
/ metabolism
Anti-Bacterial Agents
/ biosynthesis
Ferritins
/ metabolism
Bacterial Proteins
/ metabolism
Iron
/ metabolism
Anthraquinones
/ metabolism
Cytochrome b Group
/ metabolism
Gene Expression Regulation, Bacterial
Prodigiosin
/ metabolism
Reactive Oxygen Species
/ metabolism
Proteomics
Benzoisochromanequinones
Streptomyces
Antibiotic production
Bacterioferritin
Iron
Two-component systems
Journal
Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812
Informations de publication
Date de publication:
24 Aug 2024
24 Aug 2024
Historique:
received:
26
04
2024
accepted:
15
08
2024
medline:
26
8
2024
pubmed:
26
8
2024
entrez:
24
8
2024
Statut:
epublish
Résumé
Several two-component systems of Streptomyces coelicolor, a model organism used for studying antibiotic production in Streptomyces, affect the expression of the bfr (SCO2113) gene that encodes a bacterioferritin, a protein involved in iron storage. In this work, we have studied the effect of the deletion mutant ∆bfr in S. coelicolor. The ∆bfr mutant exhibits a delay in morphological differentiation and produces a lesser amount of the two pigmented antibiotics (actinorhodin and undecylprodigiosin) compared to the wild type on complex media. The effect of iron in minimal medium was tested in the wild type and ∆bfr mutant. Consequently, we also observed different levels of production of the two pigmented antibiotics between the two strains, depending on the iron concentration and the medium (solid or liquid) used. Contrary to expectations, no differences in intracellular iron concentration were detected between the wild type and ∆bfr mutant. However, a higher level of reactive oxygen species in the ∆bfr mutant and a higher tolerance to oxidative stress were observed. Proteomic analysis showed no variation in iron response proteins, but there was a lower abundance of proteins related to actinorhodin and ribosomal proteins, as well as others related to secondary metabolite production and differentiation. Additionally, a higher abundance of proteins related to various types of stress, such as respiration and hypoxia among others, was also revealed. Data are available via ProteomeXchange with identifier PXD050869. This bacterioferritin in S. coelicolor (Bfr) is a new element in the complex regulation of secondary metabolism in S. coelicolor and, additionally, iron acts as a signal to modulate the biosynthesis of active molecules. Our model proposes an interaction between Bfr and iron-containing regulatory proteins. Thus, identifying these interactions would provide new information for improving antibiotic production in Streptomyces.
Sections du résumé
BACKGROUND
BACKGROUND
Several two-component systems of Streptomyces coelicolor, a model organism used for studying antibiotic production in Streptomyces, affect the expression of the bfr (SCO2113) gene that encodes a bacterioferritin, a protein involved in iron storage. In this work, we have studied the effect of the deletion mutant ∆bfr in S. coelicolor.
RESULTS
RESULTS
The ∆bfr mutant exhibits a delay in morphological differentiation and produces a lesser amount of the two pigmented antibiotics (actinorhodin and undecylprodigiosin) compared to the wild type on complex media. The effect of iron in minimal medium was tested in the wild type and ∆bfr mutant. Consequently, we also observed different levels of production of the two pigmented antibiotics between the two strains, depending on the iron concentration and the medium (solid or liquid) used. Contrary to expectations, no differences in intracellular iron concentration were detected between the wild type and ∆bfr mutant. However, a higher level of reactive oxygen species in the ∆bfr mutant and a higher tolerance to oxidative stress were observed. Proteomic analysis showed no variation in iron response proteins, but there was a lower abundance of proteins related to actinorhodin and ribosomal proteins, as well as others related to secondary metabolite production and differentiation. Additionally, a higher abundance of proteins related to various types of stress, such as respiration and hypoxia among others, was also revealed. Data are available via ProteomeXchange with identifier PXD050869.
CONCLUSION
CONCLUSIONS
This bacterioferritin in S. coelicolor (Bfr) is a new element in the complex regulation of secondary metabolism in S. coelicolor and, additionally, iron acts as a signal to modulate the biosynthesis of active molecules. Our model proposes an interaction between Bfr and iron-containing regulatory proteins. Thus, identifying these interactions would provide new information for improving antibiotic production in Streptomyces.
Identifiants
pubmed: 39182107
doi: 10.1186/s12934-024-02510-1
pii: 10.1186/s12934-024-02510-1
doi:
Substances chimiques
Anti-Bacterial Agents
0
Ferritins
9007-73-2
Bacterial Proteins
0
Iron
E1UOL152H7
bacterioferritin
9035-38-5
Anthraquinones
0
actinorhodin
G4HH387T6Z
undecylprodigiosin
52340-48-4
Cytochrome b Group
0
Prodigiosin
OL369FU7CJ
Reactive Oxygen Species
0
Benzoisochromanequinones
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
234Subventions
Organisme : "Escalera de Excelencia" Program awarded by the Regional Government of Castile and Leon
ID : CLU-2017-03
Organisme : Grant awarded for university teacher training FPU 2022 from Spanish Ministry of Education, Culture and Sport
ID : FPU22/00747
Organisme : MCIN/AEI /10.13039/501100011033
ID : PID2019-107716RB-I00
Organisme : MCIN/AEI /10.13039/501100011033/ and by FEDER "Una manera de hacer Europa"
ID : PID2022-140962OB-I00
Organisme : Internationalization Project "CL-EI-2021-08 - IBFG Unit of Excellence " of the Spanish National Research Council (CSIC), funded by the Regional Government of Castile and Leon and the European Regional Development Fund ("Europe Drives Our Growth")
ID : CL-EI-2021-08 - IBFG Unit of Excellence
Informations de copyright
© 2024. The Author(s).
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