Article
Identification of four acidic amino acids that constitute the catalytic center of the RuvC Holliday junction resolvase.
Proceedings of the National Academy of Sciences of the United States of America - 1 Aug 1995
Saito A, Iwasaki H, Ariyoshi M, Morikawa K, Shinagawa H
Abstract excerpt
Escherichia coli RuvC protein is a specific endonuclease that resolves Holliday junctions during homologous recombination. Since the endonucleolytic activity of RuvC requires a divalent cation and since 3 or 4 acidic residues constitute the catalytic centers of several nucleases that require a divalent cation for the catalytic activity, we examined whether any of the acidic residues of RuvC were required for the...
Topics
- Aspartic Acid
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Catalysis
- DNA, Bacterial
- Endodeoxyribonucleases
- Escherichia coli
- Escherichia coli Proteins
- Genetic Complementation Test