Specificity of protein-DNA interactions in hypersaline environment: structural studies on complexes of Halobacterium salinarum oxidative stress-dependent protein hsRosR.
Archaeal Proteins
/ chemistry
Base Sequence
Binding Sites
Cloning, Molecular
Crystallography, X-Ray
DNA, Archaeal
/ chemistry
Gene Expression
Genetic Vectors
/ chemistry
Halobacterium salinarum
/ genetics
Haloferax
/ genetics
Kinetics
Models, Molecular
Nucleic Acid Conformation
Potassium Chloride
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Reactive Oxygen Species
/ metabolism
Recombinant Proteins
/ chemistry
Salt Tolerance
/ genetics
Sequence Alignment
Stress, Physiological
Thermodynamics
Transcription Factors
/ chemistry
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
19 09 2019
19 09 2019
Historique:
accepted:
02
07
2019
revised:
13
06
2019
received:
06
03
2019
pubmed:
17
7
2019
medline:
4
12
2019
entrez:
17
7
2019
Statut:
ppublish
Résumé
Interactions between proteins and DNA are crucial for all biological systems. Many studies have shown the dependence of protein-DNA interactions on the surrounding salt concentration. How these interactions are maintained in the hypersaline environments that halophiles inhabit remains puzzling. Towards solving this enigma, we identified the DNA motif recognized by the Halobactrium salinarum ROS-dependent transcription factor (hsRosR), determined the structure of several hsRosR-DNA complexes and investigated the DNA-binding process under extreme high-salt conditions. The picture that emerges from this work contributes to our understanding of the principles underlying the interplay between electrostatic interactions and salt-mediated protein-DNA interactions in an ionic environment characterized by molar salt concentrations.
Identifiants
pubmed: 31310308
pii: 5532612
doi: 10.1093/nar/gkz604
pmc: PMC7145548
doi:
Substances chimiques
Archaeal Proteins
0
DNA, Archaeal
0
Reactive Oxygen Species
0
Recombinant Proteins
0
Transcription Factors
0
Potassium Chloride
660YQ98I10
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8860-8873Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
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