The Small DdrR Protein Directly Interacts with the UmuDAb Regulator of the Mutagenic DNA Damage Response in Acinetobacter baumannii.
Acinetobacter baumannii
DNA damage
DNA repair
Induction of gene expression
LexA UmuDAb
SOS response
antibiotic resistance
bacteriophage induction
Journal
Journal of bacteriology
ISSN: 1098-5530
Titre abrégé: J Bacteriol
Pays: United States
ID NLM: 2985120R
Informations de publication
Date de publication:
15 03 2022
15 03 2022
Historique:
pubmed:
23
2
2022
medline:
22
4
2022
entrez:
22
2
2022
Statut:
ppublish
Résumé
Acinetobacter baumannii poses a great threat in health care settings worldwide, with clinical isolates displaying an ever-evolving multidrug resistance. In strains of A. baumannii, expression of multiple error-prone polymerase genes are corepressed by UmuDAb, a member of the LexA superfamily, and a small protein, DdrR. It is currently unknown how DdrR establishes this repression. Here, we used surface plasmon resonance spectrometry to show that DdrR formed a stable complex with the UmuDAb regulator. Our results indicated that the carboxy-terminal dimerization domain of UmuDAb formed the interaction interface with DdrR. Our
Identifiants
pubmed: 35191762
doi: 10.1128/jb.00601-21
pmc: PMC8923225
doi:
Substances chimiques
Bacterial Proteins
0
Mutagens
0
Transcription Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0060121Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R017689/1
Pays : United Kingdom
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