ArticleProceedings of the National Academy of Sciences of the United States of America2008
A purple acidophilic di-ferric DNA ligase from Ferroplasma.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 29 citations in OpenAlex.
- Human DNA ligase IV is able to use NAD+ as an alternative adenylation donor for DNA ends ligation.Nucleic acids research · 2019Article
- Metabolic and evolutionary patterns in the extremely acidophilic archaeon Ferroplasma acidiphilum YScientific reports · 2017Article
- Iron mediates catalysis of nucleic acid processing enzymes: support for Fe(II) as a cofactor before the great oxidation event.Nucleic acids research · 2017Article
- Archaeal Nucleic Acid Ligases and Their Potential in Biotechnology.Archaea (Vancouver, B.C.) · 2015Review
- Microbial diversity and metabolic networks in acid mine drainage habitats.Frontiers in microbiology · 2015Review
- Crystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iron and calcium-containing active site.The Journal of biological chemistry · 2014Article
- Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH optima of two carboxylesterases.The Journal of biological chemistry · 2014Article
- Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications.Extremophiles : life under extreme conditions · 2012Review
- Molecular characterization of NAD+-dependent DNA ligase from Wolbachia endosymbiont of lymphatic filarial parasite Brugia malayi.PloS one · 2012Article
- Environmental, biogeographic, and biochemical patterns of archaea of the family Ferroplasmaceae.Applied and environmental microbiology · 2011Review
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe here an extraordinary purple-colored DNA ligase, LigFa, from the acidophilic ferrous iron-oxidizing archaeon Ferroplasma acidiphilum, a di-ferric enzyme with an extremely low pH activity optimum. Unlike any other DNA ligase studied to date, LigFa contains two Fe(3+)-tyrosinate centers and lacks any requirement for either Mg(2+) or K(+) for activity. DNA ligases from closest phylogenetic and ecophysiological relatives have normal pH optima (6.0-7.5), lack iron, and require Mg(2+)/K(+) for activity. Ferric iron retention is pH-dependent, with release resulting in partial protein unfolding and loss of activity. Reduction of the Fe(3+) to Fe(2+) results in an 80% decrease in DNA substrate binding and an increase in the pH activity optimum to 5.0. DNA binding induces significant conformational change around the iron site(s), suggesting that the ferric irons of LigFa act both as structure organizing and stabilizing elements and as Lewis acids facilitating DNA binding at low pH.
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