Glycosylation of a DNA-binding protein in Salmonella enterica
Author Information
Author(s): Hanna Ebert, Maria-Cristina Roque-Barreira, Emerson S. Bernardes, Ademilson Panunto-Castelo, Marcelo V. Sousa, Igor C. Almeida, Marcelo Brocchi
Primary Institution: Universidade de São Paulo
Hypothesis
Does the DNA-binding protein Dps in Salmonella enterica undergo glycosylation?
Conclusion
The study provides evidence that Dps undergoes post-translational modifications, including glycosylation, during the early growth phases of Salmonella enterica.
Supporting Evidence
- The N-terminal sequencing of the purified Dps showed 100% identity with the Dps of Salmonella enterica.
- Monosaccharide analysis revealed the presence of mannose, glucose, and an unknown sugar residue in Dps.
- Jacalin-binding assays indicated that glycosylation affects the protein's interaction with lectins.
Takeaway
Scientists found that a protein in Salmonella that helps protect DNA is modified with sugars, which might help it work better when the bacteria are stressed.
Methodology
The Dps protein was purified using affinity chromatography and analyzed for glycosylation through various biochemical assays.
Limitations
The study does not explore the full structural details of the glycosylation or its functional implications in depth.
Digital Object Identifier (DOI)
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