Clostridioides difficile SinR' regulates toxin, sporulation and motility through protein-protein interaction with SinR.
Clostridioides difficile sin locus
Clostridium difficile
Gene regulation
SinR
motility
sporulation
toxin production
Journal
Anaerobe
ISSN: 1095-8274
Titre abrégé: Anaerobe
Pays: England
ID NLM: 9505216
Informations de publication
Date de publication:
Oct 2019
Oct 2019
Historique:
received:
30
10
2018
revised:
10
04
2019
accepted:
07
05
2019
pubmed:
12
5
2019
medline:
21
1
2020
entrez:
12
5
2019
Statut:
ppublish
Résumé
Clostridioides difficile is a Gram-positive, anaerobic bacterium. It is known that C. difficile is one of the major causes of antibiotic associated diarrhea. The enhanced antibiotic resistance observed in C. difficile is the result of highly resistant spores produced by the bacterium. In Bacillus subtilis, the sin operon is involved in sporulation inhibition. Two proteins coded within this operon, SinR and SinI, have an antagonistic relationship; SinR acts as an inhibitor to sporulation whereas SinI represses the activity of SinR, thus allowing the bacterium to sporulate. In a previous study, we examined the sin locus in C. difficile and named the two genes associated with this operon sinR and sinR', analogous to sinR and sinI in B. subtilis, respectively. We have shown that SinR and SinR' have pleiotropic roles in pathogenesis pathways and interact antagonistically with each other. Unlike B. subtilis SinI, SinR' in C. difficile carries two domains: the HTH domain and the Multimerization Domain (MD). In this study, we first performed a GST Pull-down experiment to determine the domain within SinR' that interacts with SinR. Second, the effect of these two domains on three phenotypes; sporulation, motility, and toxin production was examined. The findings of this study confirmed the prediction that the Multimerization Domain (MD) of SinR' is responsible for the interaction between SinR and SinR'. It was also discovered that SinR' regulates sporulation, toxin production and motility primarily by inhibiting SinR activity through the Multimerization Domain (MD).
Identifiants
pubmed: 31077800
pii: S1075-9964(19)30080-0
doi: 10.1016/j.anaerobe.2019.05.002
pmc: PMC6785386
mid: NIHMS1529815
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Bacterial Toxins
0
FlaD protein, Bacteria
147757-14-0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1-7Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM103418
Pays : United States
Organisme : NIGMS NIH HHS
ID : P20 GM113117
Pays : United States
Organisme : NIAID NIH HHS
ID : R03 AI135762
Pays : United States
Organisme : NIAID NIH HHS
ID : R15 AI122173
Pays : United States
Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.
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