ArticleExtremophiles : life under extreme conditions2007
Characterization of an ATP-dependent DNA ligase from the acidophilic archaeon "Ferroplasma acidarmanus" Fer1.
Article in Extremophiles : life under extreme conditions, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Metagenomic Mining for Esterases in the Microbial Community of Los Rueldos Acid Mine Drainage Formation.Frontiers in microbiology · 2022Article
- Extremophile Microbial Communities and Enzymes for Bioenergetic Application Based on Multi-Omics Tools.Current genomics · 2020Review
- Archaeal Nucleic Acid Ligases and Their Potential in Biotechnology.Archaea (Vancouver, B.C.) · 2015Review
- Protein adaptations in archaeal extremophiles.Archaea (Vancouver, B.C.) · 2013Review
- A purple acidophilic di-ferric DNA ligase from Ferroplasma.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A single amino acid substitution in the DNA-binding domain of Aeropyrum pernix DNA ligase impairs its interaction with proliferating cell nuclear antigen.Extremophiles : life under extreme conditions · 2007Article
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Authors and funding
5 authors.
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Abstract
Analysis of the genome of "Ferroplasma acidarmanus" Fer1, an archaeon that is an extreme acidophile, identified an open reading frame encoding a putative ATP-dependent DNA ligase, which we termed FaLig. The deduced amino acid sequence of FaLig contains 595 amino acids, with a predicted molecular mass of 67.8 kDa. "F. acidarmanus" Fer1 is classified as a Euryarchaeote, but phylogenetic analysis using amino acid sequences showed that FaLig is more similar to DNA ligases from Crenarchaeota, suggesting that lateral transfer of these genes has occurred among archaea. The gene sequence encoding FaLig was cloned into a bacterial expression vector harbouring an upstream His-tag to aid purification. Conditions for expression and purification from Escherichia coli were identified and recombinant FaLig was confirmed to be an ATP-dependent DNA ligase. Optimal conditions for nick-joining by the protein were pH 6-7, 0.5 mM ATP, in the presence of either Mg(2+) or Mn(2+). Using a range of nicked, double-stranded nucleic acids, ligation was detected with the same substrates as previously determined for other DNA ligases. Although FaLig is the DNA ligase from one of the most extreme acidophilic organism yet studied, this characterization suggests that its biochemical mechanism is analogous to that of enzymes from other cellular systems.
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