Cloning, expression, and characterization of a DNA ligase from a hyperthermophilic archaeon Thermococcus sp

Biotechnology Letters
Yun Jae KimJung-Hyun Lee

Abstract

Genomic analysis of a hyperthermophilic archaeon, Thermococcus sp. NA1, revealed an ORF of 1689 bases encoding 562 amino acids that showed a high similarity to DNA ligases from other hyperthermophilic archaea. The ligase, which was designated TNA1_lig (Thermococcus sp. NA1 ligase), was cloned and expressed in Escherichia coli. The recombinant TNA1_lig was purified by metal affinity chromatography. The optimum ligase activity of the recombinant TNA1_lig occurred at 80 degrees C and pH 7.5. The enzyme was activated by MgCl2 and ZnCl2 but was inhibited by MnCl2 and NiCl2. Additionally, the enzyme was activated by either ATP or NAD+.

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Dec 9, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Supangat SupangatSun-Shin Cha
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Nov 30, 2018·Nucleic Acids Research·Shih-Hsun Chen, Xiaochun Yu

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