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Genetic evidence for two protein domains and a potential new activity in bacteriophage T4 DNA polymerase.

1990; Volume: 124; Issue: 2 Linguagem: Inglês

10.1093/genetics/124.2.213

3049-7094

Linda J. Reha-Krantz,

Plant Virus Research Studies

Abstract 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.