人类核酸内切酶 III/NTH1：聚焦于 [4Fe-4S] 簇和 N 端结构域。
Human endonuclease III/NTH1: focusing on the [4Fe-4S] cluster and the N-terminal domain.
机构信息
Instituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, 2780-157, Oeiras, Portugal.
Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000, Grenoble, France.
出版信息
Chem Commun (Camb). 2022 Nov 10;58(90):12568-12571. doi: 10.1039/d2cc03643f.
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.
人类核酸内切酶 III（EndoIII），即 hNTH1，是一种含有 FeS 的酶，可修复 DNA 中氧化损伤的碱基。我们在此报告了对全长 hNTH1 和 N 端截断形式的首个比较生物物理研究，它们具有与细菌 EndoIII 同源的结构域架构。振动光谱、光谱电化学和 SAXS 实验揭示了两种酶形式的独特性质，并表明 N 端结构域对于损伤识别起始时的 DNA 结合很重要。
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