Cloning, expression, and characterization of a DNA ligase from a hyperthermophilic archaeon Thermococcus sp.
- Authors
- Kim, YJ[Kim, YJ]; Lee, HS[Lee, HS]; Bae, SS[Bae, SS]; Jeon, JH[Jeon, JH]; Yang, SH[Yang, SH]; Lim, JK[Lim, JK]; Kang, SG[Kang, SG]; Kwon, ST[Kwon, ST]; Lee, JH[Lee, JH]
- Issue Date
- Mar-2006
- Publisher
- SPRINGER
- Keywords
- Archaea; DNA ligase; Thermococcus sp.
- Citation
- BIOTECHNOLOGY LETTERS, v.28, no.6, pp.401 - 407
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOTECHNOLOGY LETTERS
- Volume
- 28
- Number
- 6
- Start Page
- 401
- End Page
- 407
- URI
- https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/87596
- DOI
- 10.1007/s10529-005-6070-6
- ISSN
- 0141-5492
- 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(+).
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Biotechnology and Bioengineering > Department of Genetic Engineering > 1. Journal Articles
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