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PublicationProceedings of the National Academy of Sciences USA
Year2008
Volume105
Pages8878-8883
International

A purple acidophilic di-ferric DNA ligase from Ferroplasma

Authors:Olga V. Golyshina , Ana Beloqui , Lars H. Böttger , José M. Andreu , Julio Polaina , Antonio López de Lacey, Alfred X. Trautwein , Kenneth N. Timmis , Peter N. Golyshin
Groups of research:BioElectroCatalysis
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 Fe3+-tyrosinate centers and lacks any requirement for either Mg2+ or K+ for activity. DNA ligases from closest phylogenetic and ecophysiological relatives have normal pH optima (6.0–7.5), lack iron, and require Mg2+/K+ for activity. Ferric iron retention is pH-dependent, with release resulting in partial protein unfolding and loss of activity. Reduction of the Fe3+ to Fe2+ 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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