Genetic Evidence for Two Protein Domains and a Potential New Activity in Bacteriophage T4 DNA Polymerase
AUTOR(ES)
Reha-Krantz, L. J.
RESUMO
Intragenic complementation was detected within the bacteriophage T4 DNA polymerase gene. Complementation was observed between specific amino (N)-terminal, temperature-sensitive (ts) mutator mutants and more carboxy (C)-terminal mutants lacking DNA polymerase polymerizing functions. Protein sequences surrounding N-terminal mutation sites are similar to sequences found in Escherichia coli ribonuclease H (RNase H) and in the 5' -> 3' exonuclease domain of E. coli DNA polymerase I. These observations suggest that T4 DNA polymerase, like E. coli DNA polymerase I, contains a discrete N-terminal domain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1203915Documentos Relacionados
- A Major Role for Bacteriophage T4 DNA Polymerase in Frameshift Mutagenesis
- Construction and characterization of a bacteriophage T4 DNA polymerase deficient in 3'-->5' exonuclease activity.
- Sequencing of Saccharomyces telomeres cloned using T4 DNA polymerase reveals two domains.
- Genetic Mapping of the Amino-Terminal Domain of Bacteriophage T4 DNA Polymerase
- Genetics and Physiology of Bacteriophage T4 3′-Phosphatase: Evidence for Involvement of the Enzyme in T4 DNA Metabolism