Article
Complementation of one RecA protein point mutation by another. Evidence for trans catalysis of ATP hydrolysis.
The Journal of biological chemistry - 5 May 2006
Cox Julia M, Abbott Stephen N, Chitteni-Pattu Sindhu, Inman Ross B, Cox Michael M
Abstract excerpt
The RecA residues Lys248 and Glu96 are closely opposed across the RecA subunit-subunit interface in some recent models of the RecA nucleoprotein filament. The K248R and E96D single mutant proteins of the Escherichia coli RecA protein each bind to DNA and form nucleoprotein filaments but do not hydrolyze ATP or dATP. A mixture of K248R and E96D single mutant proteins restores dATP hydrolysis to 25% of the wild...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Catalysis
- DNA
- Escherichia coli
- Genetic Complementation Test
- Hydrolysis
- Lysine
- Microscopy, Electron
- Molecular Conformation
- Mutation
- Point Mutation
- Rec A Recombinases