Biochemical characterization of interactions between DNA polymerase and single-stranded DNA-binding protein in bacteriophage RB69.
The Journal of biological chemistry (2003), Volume 278, Page 3876
Abstract:
Polymerases:
Topics:
Kinetic Parameters, Accessory Proteins/Complexes
One line summary:
The presence of the RB69 DNA polymerase at the primer terminus results in a 57-fold increase in gp32 (SSB) affinity for ssDNA as a result of DNA polymerase:SSB cooperativity.
Status:
new | topics/pols set | partial results | complete | validated |
Results:
Polymerase | Reference | Property | Result | Context |
---|---|---|---|---|
RB69 D222AD327A | Biochemical characterization of interactions between DNA polymerase and single-stranded DNA-binding protein in bacteriophage RB69. | Kd | 124nM | Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: fluorescence titration |
RB69 D222AD327A | Biochemical characterization of interactions between DNA polymerase and single-stranded DNA-binding protein in bacteriophage RB69. | Kd | 353nM | Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: fluorescence titration (gp32 added) |