Article
Escherichia coli Dps interacts with DnaA protein to impede initiation: a model of adaptive mutation.
Molecular microbiology - 1 Mar 2008
Chodavarapu Sundari, Gomez Ruben, Vicente Matias, Kaguni Jon M
Abstract excerpt
During exponential growth, the level of Dps transiently increases in response to oxidative stress to sequester and oxidize Fe2+, which would otherwise lead to hydroxyl radicals that damage the bacterial chromosome. We report that Dps specifically interacts with DnaA protein by affinity chromatography and a solid phase binding assay, requiring the N-terminal region of DnaA to interact. In vitro, Dps inhibits DnaA...
Topics
- Bacterial Outer Membrane Proteins
- Bacterial Proteins
- DNA Replication
- DNA-Binding Proteins
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression Regulation, Bacterial
- Magnesium
- Mutation
- Protein Binding