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

Reha-Krantz LJ
Genetics (1990), Volume 124, Page 213
PubMed entry Full article text


Intragenic complementation was detected within the bacteriophage T4 ...
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.



Structure and Structure/Function, Alignments

One line summary:

T4 DNA polymerase has a distinct N-terminal domain.


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