Article
Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction.
Journal of bacteriology - 1 Oct 1995
Brosh R M, Matson S W
Abstract excerpt
Site-directed mutagenesis has been employed to address the functional significance of the highly conserved aspartic and glutamic acid residues present in the Walker B (also called motif II) sequence in Escherichia coli DNA helicase II. Two mutant proteins, UvrDE221Q and UvrDD220NE221Q, were expre...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Aspartic Acid
- Base Sequence
- DNA
- DNA Helicases
- DNA Repair
- DNA, Single-Stranded
- Escherichia coli
- Escherichia coli Proteins
- Genes, Dominant
- Glutamic Acid
- Kinetics
- Molecular Sequence Data
- Mutation
- Phenotype
- Sequence Deletion