Article
The highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-Ser in alpha-like DNA polymerases is required by phage phi 29 DNA polymerase for protein-primed initiation and polymerization.
Proceedings of the National Academy of Sciences of the United States of America - 1 Jun 1990
Bernad A, Lázaro J M, Salas M, Blanco L
Abstract excerpt
The alpha-like DNA polymerases from bacteriophage phi 29 and other viruses, prokaryotes and eukaryotes contain an amino acid consensus sequence that has been proposed to form part of the dNTP binding site. We have used site-directed mutants to study five of the six highly conserved consecutive amino acids corresponding to the most conserved C-terminal segment (Tyr-Gly-Asp-Thr-Asp-Ser). Our results indicate that...
Topics
- Amino Acid Sequence
- Binding Sites
- Coliphages
- DNA Polymerase II
- DNA Replication
- DNA-Directed DNA Polymerase
- Escherichia coli
- Exodeoxyribonuclease V
- Exodeoxyribonucleases
- Kinetics