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Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair.

Zhu C, Lu L, Zhang J, Yue Z, Song J, Zong S, Liu M, Stovicek O, Gao YQ, Yi C
Proc Natl Acad Sci U S A 113 7792-7 (2016)
Related entries: 5itq, 5itr, 5itt, 5itu, 5itx

Cited: 33 times
EuropePMC logo PMID: 27354518

Abstract

NEIL1 (Nei-like 1) is a DNA repair glycosylase guarding the mammalian genome against oxidized DNA bases. As the first enzymes in the base-excision repair pathway, glycosylases must recognize the cognate substrates and catalyze their excision. Here we present crystal structures of human NEIL1 bound to a range of duplex DNA. Together with computational and biochemical analyses, our results suggest that NEIL1 promotes tautomerization of thymine glycol (Tg)-a preferred substrate-for optimal binding in its active site. Moreover, this tautomerization event also facilitates NEIL1-catalyzed Tg excision. To our knowledge, the present example represents the first documented case of enzyme-promoted tautomerization for efficient substrate recognition and catalysis in an enzyme-catalyzed reaction.

Reviews - 5ity mentioned but not cited (2)

  1. The involvement of nucleotide excision repair proteins in the removal of oxidative DNA damage. Kumar N, Raja S, Van Houten B. Nucleic Acids Res 48 11227-11243 (2020)
  2. Emerging Roles of DNA Glycosylases and the Base Excision Repair Pathway. Mullins EA, Rodriguez AA, Bradley NP, Eichman BF. Trends Biochem Sci 44 765-781 (2019)

Articles - 5ity mentioned but not cited (7)



Reviews citing this publication (7)

  1. Base excision repair of oxidative DNA damage: from mechanism to disease. Whitaker AM, Schaich MA, Smith MR, Flynn TS, Freudenthal BD. Front Biosci (Landmark Ed) 22 1493-1522 (2017)
  2. Occurrence, Biological Consequences, and Human Health Relevance of Oxidative Stress-Induced DNA Damage. Yu Y, Cui Y, Niedernhofer LJ, Wang Y. Chem Res Toxicol 29 2008-2039 (2016)
  3. Repair of 8-oxo-7,8-dihydroguanine in prokaryotic and eukaryotic cells: Properties and biological roles of the Fpg and OGG1 DNA N-glycosylases. Boiteux S, Coste F, Castaing B. Free Radic Biol Med 107 179-201 (2017)
  4. Formation and processing of DNA damage substrates for the hNEIL enzymes. Fleming AM, Burrows CJ. Free Radic Biol Med 107 35-52 (2017)
  5. Hide and seek: How do DNA glycosylases locate oxidatively damaged DNA bases amidst a sea of undamaged bases? Lee AJ, Wallace SS. Free Radic Biol Med 107 170-178 (2017)
  6. Structural Aspects of DNA Repair and Recombination in Crop Improvement. Verma P, Tandon R, Yadav G, Gaur V. Front Genet 11 574549 (2020)
  7. Noncatalytic Domains in DNA Glycosylases. Torgasheva NA, Diatlova EA, Grin IR, Endutkin AV, Mechetin GV, Vokhtantsev IP, Yudkina AV, Zharkov DO. Int J Mol Sci 23 7286 (2022)

Articles citing this publication (17)



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