| Product Name |
Deinococcus proteolyticus Single-Stranded DNA-Binding Protein (DprSSB) |
| Overview |
The single-stranded DNA-binding protein from Deinococcus proteolyticus (DprSSB) is a thermostable, homodimeric SSB essential for DNA replication, recombination, and repair in this extremophilic bacterium. Like other SSBs from the Deinococcus-Thermus group, DprSSB is structurally unique among bacterial SSBs: each monomer contains two oligonucleotide/oligosaccharide-binding (OB) folds, and the functional unit is a symmetric dimer. This arrangement results in a four-OB-fold DNA-binding surface, distinct from the homotetrameric, single-OB-fold-per-monomer SSBs found in most bacteria[1][2][5][6][8]. DprSSB binds single-stranded DNA with high affinity, protects it from degradation, and prevents secondary structure formation. It is also implicated in supporting RecA-mediated strand exchange and DNA repair, a hallmark of the robust genome maintenance systems in Deinococcus species.
|
| Size |
100 µg |
| Concentration |
1 mg/mL |
| Molecular Weight |
~31 kDa (monomer); ~62 kDa (homodimer functional unit)[8] |
| Key Features |
- Homodimeric structure, each monomer with two OB folds (four OB folds per dimer)[1][2][6][8]
- Thermostable and active at elevated temperatures
- High-affinity binding to single-stranded DNA; protects ssDNA and prevents secondary structure formation
- Supports RecA-mediated DNA strand exchange and DNA repair pathways
- Contributes to the extraordinary DNA damage resistance of Deinococcus species
|
| Applications |
- Stabilization of ssDNA in high-temperature molecular biology assays
- Studies of DNA replication, recombination, and repair in extremophiles
- Model system for investigating unique SSB architectures and DNA-protein interactions
|
| Source |
Recombinant protein expressed in E. coli |
| Quality Control |
- Purity >95% by SDS-PAGE
- Functional validation in ssDNA binding assays
|
| Formulation |
20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 10% glycerol, pH 7.5 |
| Storage |
-80 °C (long-term); avoid repeated freeze-thaw cycles |
| References |
- Bernstein, D.A., et al. Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein. Proc Natl Acad Sci USA. 2004; 101(7): 2273–2278.[1][2]
- George, N.P., et al. Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA-binding protein-DNA complexes. J Biol Chem. 2012; 287(29): 24570–24582.[5][7]
- Yamamoto, K., et al. Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins. J Biochem. 2007; 141(5): 653–661.[8]
- Suzuki, S., et al. The essential role of the Deinococcus radiodurans ssb gene in cell survival after irradiation and oxidative stress. PLoS ONE. 2013; 8(8): e71651.[6]
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