Article
Y265H mutator mutant of DNA polymerase beta. Proper teometric alignment is critical for fidelity.
The Journal of biological chemistry - 6 Apr 2001
Shah A M, Li S X, Anderson K S, Sweasy J B
Abstract excerpt
DNA polymerases have the unique ability to select a specific deoxynucleoside triphosphate from a pool of similarly structured substrates. One of these enzymes, DNA polymerase beta, offers a simple system to relate polymerase structure to the fidelity of DNA synthesis. In this study, a mutator DNA polymerase beta, Y265H, was identified using an in vivo genetic screen. Purified Y265H produced errors at a 40-fold...
Topics
- Bacterial Proteins
- DNA Polymerase beta
- Mutation
- Protein Conformation
- Structure-Activity Relationship