Article
The conserved active site motif A of Escherichia coli DNA polymerase I is highly mutable.
The Journal of biological chemistry - 1 Jun 2001
Shinkai A, Patel P H, Loeb L A
Abstract excerpt
Escherichia coli DNA polymerase I participates in DNA replication, DNA repair, and genetic recombination; it is the most extensively studied of all DNA polymerases. Motif A in the polymerase active site has a required role in catalysis and is highly conserved. To assess the tolerance of motif A for amino acid substitutions, we determined the mutability of the 13 constituent amino acids Val(700)-Arg(712) by using...
Topics
- Amino Acid Motifs
- Amino Acid Sequence
- Aspartic Acid
- Binding Sites
- Catalysis
- Conserved Sequence
- DNA Polymerase I
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Evolution, Molecular
- Isoleucine
- Kinetics
- Molecular Sequence Data
- Mutagenesis
- Mutagenesis, Site-Directed
- Mutation
- RNA
- Sequence Analysis, DNA