Revealing the DNA Binding Modes of CsoR by EPR Spectroscopy.
Journal
ACS omega
ISSN: 2470-1343
Titre abrégé: ACS Omega
Pays: United States
ID NLM: 101691658
Informations de publication
Date de publication:
24 Oct 2023
24 Oct 2023
Historique:
received:
25
08
2023
accepted:
28
09
2023
medline:
30
10
2023
pubmed:
30
10
2023
entrez:
30
10
2023
Statut:
epublish
Résumé
In pathogens, a unique class of metalloregulator proteins, called gene regulatory proteins, sense specific metal ions that initiate gene transcription of proteins that export metal ions from the cell, thereby preventing toxicity and cell death. CsoR is a metalloregulator protein found in various bacterial systems that "sense" Cu(I) ions with high affinity. Upon copper binding, CsoR dissociates from the DNA promoter region, resulting in initiation of gene transcription. Crystal structures of CsoR in the presence and absence of Cu(I) from various bacterial systems have been reported, suggesting either a dimeric or tetrameric structure of these helical proteins. However, structural information about the CsoR-DNA complex is missing. Here, we applied electron paramagnetic resonance (EPR) spectroscopy to follow the conformational and dynamical changes that
Identifiants
pubmed: 37901548
doi: 10.1021/acsomega.3c06336
pmc: PMC10601412
doi:
Types de publication
Journal Article
Langues
eng
Pagination
39886-39895Informations de copyright
© 2023 The Authors. Published by American Chemical Society.
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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