Binding of the Dimeric Deinococcus radiodurans Single-Stranded DNA Binding Protein to Single-Stranded DNA

Binding of the Dimeric Deinococcus radiodurans Single-Stranded DNA Binding Protein to Single-Stranded DNA

Deinococcus radiodurans single-stranded (ss) DNA binding protein (DrSSB) originates from a radiation-resistant bacterium and participates in DNA recombination, replication, and repair. Although it functions as a homodimer, it contains four DNA binding domains (OB-folds) and thus is structurally simi...

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Veröffentlicht in:Biochemistry (Easton) 2010-09, Vol.49 (38), p.8266-8275
Hauptverfasser: Kozlov, Alexander G, Eggington, Julie M, Cox, Michael M, Lohman, Timothy M
Format: Artikel
Sprache:eng
Schlagworte:
Bacterial Proteins - metabolism
Binding Sites
Calorimetry
Deinococcus - genetics
Deinococcus - metabolism
DNA, Single-Stranded - chemistry
DNA, Single-Stranded - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Poly T - metabolism
Protein Binding
Sodium Chloride - chemistry
Sodium Chloride - metabolism
Temperature
Thermodynamics
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Zusammenfassung:Deinococcus radiodurans single-stranded (ss) DNA binding protein (DrSSB) originates from a radiation-resistant bacterium and participates in DNA recombination, replication, and repair. Although it functions as a homodimer, it contains four DNA binding domains (OB-folds) and thus is structurally similar to the Escherichia coli SSB (EcoSSB) homotetramer. We examined the equilibrium binding of DrSSB to ssDNA for comparison with that of EcoSSB. We find that the occluded site size of DrSSB on poly(dT) is ∼45 nucleotides under low-salt conditions (
ISSN:0006-2960
1520-4995
DOI:10.1021/bi100920w