Genetic evidence for two protein domains and a potential new activity in bacteriophage T4 DNA polymerase.
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.
Reha-Krantz
L J
LJ
Department of Genetics, University of Alberta, Edmonton, Canada.
D000595:Amino Acid Sequence; D002499:Centrifugation, Density Gradient; D004279:DNA, Viral / Q000096:biosynthesis / Q000235:genetics; D004259:DNA-Directed DNA Polymerase / Q000235:genetics* / Q000378:metabolism; D005814:Genes, Viral; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D009154:Mutation; D012689:Sequence Homology, Nucleic Acid; D013604:T-Phages / Q000201:enzymology / Q000235:genetics*; D013696:Temperature
D004279:DNA, Viral; D004259:DNA-Directed DNA Polymerase