The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli.
Open accessAbstract
A starvation-inducible DNA-binding protein was discovered as a result of the analysis of proteins synthesized in 3-day-old cultures of Escherichia coli. This 19-kD protein, designated Dps, is abundant in starved cells. In vitro, Dps forms extremely stable complexes with DNA, without apparent sequence specificity. When complexed with Dps, DNA is rendered DNase resistant. Mutant cells lacking Dps show dramatic changes in the pattern of proteins synthesized during starvation. The mutants also fail to develop starvation-induced resistance to hydrogen peroxide, an agent that can cause oxidative damage to DNA in vivo. These results have prompted us to postulate that Dps plays an important role both in gene expression and DNA protection during stationary phase. The existence of similar proteins, heretofore with no known function, in bacterial species distantly related to Escherichia coli suggests that Dps may define a novel class of widely conserved DNA-binding proteins.
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Cites
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Oxidative Stress Resistance in Deinococcus radiodurans
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Intracellular Copper Does Not Catalyze the Formation of Oxidative DNA Damage in Escherichia coli
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Metadata
- Authors
- Almiron, M., Link, A. J., Furlong, D., & Kolter, R.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1992-12-01
- Volume
- 6
- Issue
- 12b
- Pages
- 2646-2654
- ISSN
- 0890-9369 (ISSN-L)
- OpenAlex
- W2127558534
- Cited by
- 773
- References
- 44
- Type
- posted content
- Language
- en
- Open access
- diamond
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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