Cloning, Expression, and Characterization of a DNA Ligase from a Hyperthermophilic Archaeon Thermococcus Sp.

Author： Kim Yun   Lee Hyun   Bae Seung   Jeon Jung   Yang Sung   Lim Jae   Kang Sung   Kwon Suk-Tae   Lee Jung-Hyun  

Publisher： Springer Publishing Company

ISSN： 0141-5492

Source： Biotechnology Letters, Vol.28, Iss.6, 2006-03, pp. : 401-407

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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 °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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