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The three Endonuclease III variants of Deinococcus radiodurans possess distinct and complementary DNA repair activities.

Authors
  • Sarre, Aili1
  • Stelter, Meike2
  • Rollo, Filipe3
  • De Bonis, Salvatore2
  • Seck, Anna4
  • Hognon, Cécilia5
  • Ravanat, Jean-Luc6
  • Monari, Antonio5
  • Dehez, François5
  • Moe, Elin7
  • Timmins, Joanna8
  • 1 The Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT the Arctic University of Norway, N-9037 Tromsø, Norway. , (Norway)
  • 2 Univ. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France. , (France)
  • 3 Instituto de Tecnologia Quimica e Biologica (ITQB), Universidade Nova de Lisboa, Av da Republica (EAN), 2780-157 Oeiras, Portugal. , (Portugal)
  • 4 Univ. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France; Univ. Grenoble Alpes, CEA, CNRS, INAC, SyMMES UMR 5819, Grenoble, France. , (France)
  • 5 LPCT, UMR 7019, Université de Lorraine, CNRS, Vandoeuvre-les-Nancy, France. , (France)
  • 6 Univ. Grenoble Alpes, CEA, CNRS, INAC, SyMMES UMR 5819, Grenoble, France. , (France)
  • 7 The Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT the Arctic University of Norway, N-9037 Tromsø, Norway; Instituto de Tecnologia Quimica e Biologica (ITQB), Universidade Nova de Lisboa, Av da Republica (EAN), 2780-157 Oeiras, Portugal. Electronic address: [email protected] , (Norway)
  • 8 Univ. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France. Electronic address: [email protected] , (France)
Type
Published Article
Journal
DNA repair
Publication Date
Mar 28, 2019
Volume
78
Pages
45–59
Identifiers
DOI: 10.1016/j.dnarep.2019.03.014
PMID: 30959406
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Endonuclease III (EndoIII) is a bifunctional DNA glycosylase that removes oxidized pyrimidines from DNA. The genome of Deinococcus radiodurans encodes for an unusually high number of DNA glycosylases, including three EndoIII enzymes (drEndoIII1-3). Here, we compare the properties of these enzymes to those of their well-studied homologues from E. coli and human. Our biochemical and mutational data, reinforced by MD simulations of EndoIII-DNA complexes, reveal that drEndoIII2 exhibits a broad substrate specificity and a catalytic efficiency surpassing that of its counterparts. In contrast, drEndoIII1 has much weaker and uncoupled DNA glycosylase and AP-lyase activities, a characteristic feature of eukaryotic DNA glycosylases, and was found to present a relatively robust activity on single-stranded DNA substrates. To our knowledge, this is the first report of such an activity for an EndoIII. In the case of drEndoIII3, no catalytic activity could be detected, but its ability to specifically recognize lesion-containing DNA using a largely rearranged substrate binding pocket suggests that it may play an alternative role in genome maintenance. Overall, these findings reveal that D. radiodurans possesses a unique set of DNA repair enzymes, including three non-redundant EndoIII variants with distinct properties and complementary activities, which together contribute to genome maintenance in this bacterium. Copyright © 2019 The Authors. Published by Elsevier B.V. All rights reserved.

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