1. Human endonuclease III/NTH1: focusing on the [4Fe-4S] cluster and the N-terminal domain
- Author
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Elin Moe, Célia M. Silveira, Lidia Zuccarello, Filipe Rollo, Meike Stelter, Salvatore De Bonis, Catharina Kulka-Peschke, Sagie Katz, Peter Hildebrandt, Ingo Zebger, Joanna Timmins, Smilja Todorovic, Instituto de Tecnologia Química e Biológica António Xavier (ITQB), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Institut für Chemie [TUB Berlin], Technical University of Berlin / Technische Universität Berlin (TU), and European Project: GA 810856
- Subjects
Iron-Sulfur Proteins ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,DNA Repair ,Metals and Alloys ,General Chemistry ,DNA ,Endonucleases ,Catalysis ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,Deoxyribonuclease (Pyrimidine Dimer) ,X-Ray Diffraction ,Scattering, Small Angle ,Materials Chemistry ,Ceramics and Composites ,Humans - Abstract
International audience; Human Endonuclease III (EndoIII), hNTH1, is an FeS containing enzyme which repairs oxidation damaged bases in DNA. We report here the first comparative biophysical study of full-length and an N-terminally truncated hNTH1, with a domain architecture homologous to bacterial EndoIII. Vibrational spectroscopy, spectroelectrochemistry and SAXS experiments reveal distinct properties of the two enzyme forms, and indicate that the N-terminal domain is important for DNA binding at the onset of damage recognition
- Published
- 2022
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