The Structure of T. aquaticus DNA Polymerase III Is Distinct from Eukaryotic Replicative DNA Polymerases

Scott Bailey, Richard A. Wing, Thomas A. Steitz

Research output: Contribution to journalArticlepeer-review

Abstract

The crystal structure of Thermus aquaticus DNA polymerase III α subunit reveals that the structure of the catalytic domain of the eubacterial replicative polymerase is unrelated to that of the eukaryotic replicative polymerase but rather belongs to the Polβ-like nucleotidyltransferase superfamily. A model of the polymerase complexed with both DNA and β-sliding clamp interacting with a reoriented binding domain and internal β binding site was constructed that is consistent with existing biochemical data. Within the crystal, two C-terminal domains are interacting through a surface that is larger than many dimer interfaces. Since replicative polymerases of eubacteria and eukaryotes/archaea are not homologous, the nature of the replicative polymerase in the last common ancestor is unknown. Although other possibilities have been proposed, the plausibility of a ribozyme DNA polymerase should be considered.

Original languageEnglish (US)
Pages (from-to)893-904
Number of pages12
JournalCell
Volume126
Issue number5
DOIs
StatePublished - Sep 8 2006
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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