The amino acid sequence required for 5' → 3' exonuclease activity of Bacillus caldotenax DNA polymerase

1 November 1995

journal article
research article
Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection

Vol. 8 (11) , 1171-1175
https://doi.org/10.1093/protein/8.11.1171

Abstract

We studied the 5' ↑ 3' exonuclease activity of Bacillus caldotenax DNA polymerase by site-directed mutagenesis. Among seven mutants constructed, two mutant DNA polymerases with an amino acid substitution of Glyl84 ↑ Asp or Glyl92 ↑ Asp were confirmed to be deficient in this exonuclease. The two positions corresponded to those of the Escherichia coli DNA polymerase I mutants defective in 5' ↑ 3' exonuclease, polA480ex and polA214. These results provide experimental support for the proposed amino acid sequence essential for the 5' ↑ 3' exonuclease activity associated with eubacterial polymerase I–like DNA polymerases (family A), including E.coli and Thermits aquaticus.

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