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Papers In Press, published online ahead of print February 21, 2002
J. Biol. Chem, 10.1074/jbc.M110198200
Submitted on October 23, 2001
Revised on February 21, 2002
Accepted on February 20, 2002
Laboratory of DNA Replication, The Rockefeller University, New York, New York 10021
Corresponding Author: odonnel{at}rockvax.rockefeller.edu
This report takes a proteomic/genomic approach to characterize the DNA polymerase III replication apparatus of the extreme thermophile, Aquifex aeolicus. Genes (dnaX, holA, holB) encoding the subunits required for clamp loading activity (t, d, d') were identified. The dnaX gene produces only the full-length product, t, and therefore differs from E. coli dnaX which produces two proteins (g and t). Nonetheless, the A. aeolicus proteins form a tdd' complex. The dnaN gene encoding the b clamp was identified and the tdd' complex is active in loading b onto DNA. A. aeolicus contains one dnaE homologue, encoding the a subunit of DNA polymerase III. Like E. coli, A. aeolicus a and t interact, although the interaction is not as tight as the a-t contact in E. coli. In addition, the A. aeolicus homologue to dnaQ, encoding the e proofreading 3'-5' exonuclease, interacts with a but does not form a stabile aoe complex, suggesting a need for a brace or bridging protein to tightly couple the polymerase and exonuclease in this system. Despite these differences to the E. coli system, the A. aeolicus proteins function to yield a robust replicase that retains significant activity at 90ºC. Similarities and differences between the A. aeolicus and E. coli Pol III systems are discussed, as is application of thermostable Pol III to biotechnology.
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