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

Yoshizumi Ishino; Asako Takahashi-Fujii; Takashi Uemori; Mitsuo Imamura; Ikunoshin Kato

doi:10.1093/protein/8.11.1171

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

Yoshizumi Ishino, Asako Takahashi-Fujii, Takashi Uemori, Mitsuo Imamura, Ikunoshin Kato

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1171-1175
Number of pages	5
Journal	Protein Engineering, Design and Selection
Volume	8
Issue number	11
DOIs	https://doi.org/10.1093/protein/8.11.1171
Publication status	Published - Nov 1 1995
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Biochemistry
Molecular Biology

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10.1093/protein/8.11.1171

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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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AU - Ishino, Yoshizumi

AU - Takahashi-Fujii, Asako

AU - Uemori, Takashi

AU - Imamura, Mitsuo

AU - Kato, Ikunoshin

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

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