Guanine glycation repair by DJ-1/Park7 and its bacterial homologs

Author:

Richarme Gilbert12ORCID,Liu Cailing3,Mihoub Mouadh1,Abdallah Jad14ORCID,Leger Thibaut5,Joly Nicolas6,Liebart Jean-Claude1,Jurkunas Ula V.3ORCID,Nadal Marc7,Bouloc Philippe8ORCID,Dairou Julien2,Lamouri Aazdine9ORCID

Affiliation:

1. Stress Molecules, Institut Jacques Monod, Université Paris Diderot—UMR7592, 15 rue Hélène Brion, 75013 Paris, France.

2. Chimie et Biochimie Pharmacologiques et Toxicologiques, Université Paris Descartes—Sorbonne Paris Cité, UMR 8601, 75270 Paris, France.

3. Schepens Eye Research Institute, Massachusetts Eye and Ear Infirmary, Department of Ophthalmology, Harvard Medical School, Boston, MA 02114, USA.

4. School of Pharmacy, Lebanese American University, Byblos, 2038 1401 Lebanon.

5. Proteomics Facility, Institut Jacques Monod, Université Paris Diderot—UMR7592, 75013 Paris, France.

6. Cellular Cycle and Development, Institut Jacques Monod, Université Paris Diderot—UMR7592, 75013 Paris, France.

7. Institut Jacques Monod, CNRS—Université Paris Diderot—UMR7592, 75013 Paris, France.

8. Institute for Integrative Biology of the Cell (I2BC), Commissariat à l'Energie Atomique et aux Energies Alternatives, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette, France.

9. Interfaces, Traitements, Organisation et Dynamique des Systèmes (ITODYS), Université Paris Diderot, UMR 7086, 15 rue J.-A. de Baïf, 75013 Paris, France.

Abstract

Not-so-sweet DNA damage repaired Glyoxal and methylglyoxal, by-products of sugar metabolism that are present in all cells, can react with, and thus damage, DNA. Indeed, glycation of guanine (G) is as prevalent as the major product of oxidative damage in DNA, 8-oxo-dG. Richarme et al. show that both prokaryotes and eukaryotes have dedicated systems that specifically repair glycation damage (see the Perspective by Dingler and Patel). The parkinsonism-associated protein DJ-1/Park7 and its bacterial homologs Hsp31, YhbO, and YajL direct the enzymatic repair of damaged glycated bases in DNA. The proteins also clean up the more vulnerable pool of free nucleotides in the cell, which are more susceptible to glycation than the nucleotides within DNA. Science , this issue p. 208 ; see also p. 130

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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