Retention of replication fidelity by a DNA polymerase functioning in a distantly related environment

Holly Kloos Dressman, Chien Chia Wang, Jim D. Karam, John W. Drake

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


The primary structures of the replicative DNA polymerases (gp43s) of bacteriophage T4 and its distant phylogenetic relative RB69 are diverged, retaining only 61% identity and 74% similarity. Nevertheless, RB69 gp43 substitutes effectively for T4 gp43 in T4 DNA replication in vivo. We show here that RB69 gp43 replicates T4 genomes in vivo with a fidelity similar to that achieved by T4 gp43. Furthermore, replication by RB69 gp43 in the distantly related environment does not enhance the mutator activities of mutations in T4 genes that encode other components of the multienzyme DNA replicase. We also show that the fidelities of RB69 gp43 and T4 gp43 are both high in vitro and that they are similarly and sharply reduced in vivo by mutations that eliminate the 3'-exonucleolytic proofreading function. We conclude that gp43 interactions with the other replication proteins are probably nonessential for polymerase fidelity.

Original languageEnglish
Pages (from-to)8042-8046
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number15
StatePublished - 22 Jul 1997


  • Bacteriophage RB69
  • Bacteriophage T4
  • DNA polymerase
  • Replication fidelity


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