Genetics, Vol 124, 213-220, Copyright © 1990


INVESTIGATIONS

Genetic Evidence for Two Protein Domains and a Potential New Activity in Bacteriophage T4 DNA Polymerase

L. J. Reha-Krantz
Department of Genetics, University of Alberta, Edmonton, Alberta, Canada T6G 2E9

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.


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