Human endonuclease III/NTH1: focusing on the [4Fe–4S] cluster and the N-terminal domain

Elin Moe (1) , Célia Silveira (1) , Lidia Zuccarello (1) , Filipe Rollo (1) , Meike Stelter (2) , Salvatore de Bonis (2) , Catharina Kulka-Peschke (3) , Sagie Katz (3) , Peter Hildebrandt (3) , Ingo Zebger (3) , Joanna Timmins (2) , Smilja Todorovic (1)

1 ITQB - Instituto de Tecnologia Química e Biológica António Xavier
2 IBS - UMR 5075 - Institut de biologie structurale
3 Institut für Chemie [TUB Berlin]

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

Domaines: Biologie structurale [q-bio.BM]

Elin Moe, Célia Silveira, Lidia Zuccarello, Filipe Rollo, Meike Stelter, et al.. Human endonuclease III/NTH1: focusing on the [4Fe–4S] cluster and the N-terminal domain. Chemical Communications, 2022, ⟨10.1039/d2cc03643f⟩. ⟨hal-03845005⟩