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      Biochemical and functional characterization of an endonuclease III from Thermococcus barophilus Ch5.

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          Abstract

          Endonuclease III (EndoIII) is a bifunctional DNA glycosylase that is essential to excise thymine glycol (Tg) from DNA. Although EndoIII is widespread in bacteria, eukarya and Archaea, our understanding on archaeal EndoIII function remains relatively incomplete due to the limited reports. Herein, we characterized an EndoIII from the hyperthermophilic euryarchaeon Thermococcus barophilus Ch5 (Tba-EndoIII) biochemically, demonstrating that the enzyme can excise Tg from dsDNA and display maximum activity at 50 ~ 70 °C and at pH 6.0 ~ 9.0 without the requirement of a divalent metal ion. Importantly, Tba-EndoIII differs from other reported archaeal EndoIII homologues in thermostability and salt requirement. As observed in other EndoIII homologues, the conserved residues D155 and H157 in Helix-hairpin-Helix motif of Tba-EndoIII are essential for Tg excision. Intriguingly, we first dissected that the conserved residues C215 and C221 in the Fe-S cluster loop in Tba-EndoIII are involved in intermediate formation and Tg excision. Additionally, we first revealed that the conserved residue L48 is flexible for intermediate formation and AP cleavage, but plays no detectable role in Tg excision. Overall, our work has revealed additional archaeal EndoIII function and catalytic mechanism.

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          Author and article information

          Journal
          World J Microbiol Biotechnol
          World journal of microbiology & biotechnology
          Springer Science and Business Media LLC
          1573-0972
          0959-3993
          Jun 25 2022
          : 38
          : 8
          Affiliations
          [1 ] College of Environmental Science and Engineering, Marine Science and Technology Institute, Yangzhou University, Yangzhou, China.
          [2 ] College of Environmental Science and Engineering, Marine Science and Technology Institute, Yangzhou University, Yangzhou, China. lkzhang@yzu.edu.cn.
          [3 ] Guangling College, Yangzhou University, Yangzhou, China. lkzhang@yzu.edu.cn.
          Article
          10.1007/s11274-022-03328-y
          10.1007/s11274-022-03328-y
          35750964
          b23f4a12-0563-423c-ac5b-ae3ad3f693f7
          History

          Endonuclease III,Hyperthermophilic Archaea,DNA damage,Base excision repair

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