Guanine glycation repair by DJ-1/Park7 and its bacterial homologs
DNA damage induced by reactive carbonyls (mainly methylglyoxal and glyoxal), called DNA glycation, is quantitatively as important as oxidative damage. DNA glycation is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity. However, in contrast to guanine oxidation repair,...
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| مؤلفون آخرون: | , , , , , , |
| التنسيق: | article |
| منشور في: |
2017
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| الوصول للمادة أونلاين: | http://hdl.handle.net/10725/10677 https://doi.org/10.1126/science.aag1095 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php https://science.sciencemag.org/content/357/6347/208/tab-article-info |
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| _version_ | 1864513487076589568 |
|---|---|
| author | Richarme, Gilbert |
| author2 | Liu, Cailing Mihoub, Mouadh Abdallah, Jad Leger, Thibaut Joly, Nicolas Liebart, Jean-Claude Jurkun, Ula V. |
| author2_role | author author author author author author author |
| author_facet | Richarme, Gilbert Liu, Cailing Mihoub, Mouadh Abdallah, Jad Leger, Thibaut Joly, Nicolas Liebart, Jean-Claude Jurkun, Ula V. |
| author_role | author |
| dc.creator.none.fl_str_mv | Richarme, Gilbert Liu, Cailing Mihoub, Mouadh Abdallah, Jad Leger, Thibaut Joly, Nicolas Liebart, Jean-Claude Jurkun, Ula V. |
| dc.date.none.fl_str_mv | 2017 2019-05-28T10:34:13Z 2019-05-28T10:34:13Z 2019-05-28 |
| dc.identifier.none.fl_str_mv | 0036-8075 http://hdl.handle.net/10725/10677 https://doi.org/10.1126/science.aag1095 Richarme, G., Liu, C., Mihoub, M., Abdallah, J., Leger, T., Joly, N., ... & Dairou, J. (2017). Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science, 357(6347), 208-211. http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php https://science.sciencemag.org/content/357/6347/208/tab-article-info |
| dc.language.none.fl_str_mv | en |
| dc.relation.none.fl_str_mv | Science |
| dc.rights.*.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.title.none.fl_str_mv | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | DNA damage induced by reactive carbonyls (mainly methylglyoxal and glyoxal), called DNA glycation, is quantitatively as important as oxidative damage. DNA glycation is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity. However, in contrast to guanine oxidation repair, how glycated DNA is repaired remains undetermined. Here, we found that the parkinsonism-associated protein DJ-1 and its bacterial homologs Hsp31, YhbO, and YajL could repair methylglyoxal- and glyoxal-glycated nucleotides and nucleic acids. DJ-1–depleted cells displayed increased levels of glycated DNA, DNA strand breaks, and phosphorylated p53. Deglycase-deficient bacterial mutants displayed increased levels of glycated DNA and RNA and exhibited strong mutator phenotypes. Thus, DJ-1 and its prokaryotic homologs constitute a major nucleotide repair system that we name guanine glycation repair. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | LAURepo_d98aabe8be2854551b7b6a0ed2cbf527 |
| identifier_str_mv | 0036-8075 Richarme, G., Liu, C., Mihoub, M., Abdallah, J., Leger, T., Joly, N., ... & Dairou, J. (2017). Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science, 357(6347), 208-211. |
| language_invalid_str_mv | en |
| network_acronym_str | LAURepo |
| network_name_str | Lebanese American University repository |
| oai_identifier_str | oai:laur.lau.edu.lb:10725/10677 |
| publishDate | 2017 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| spelling | Guanine glycation repair by DJ-1/Park7 and its bacterial homologsRicharme, GilbertLiu, CailingMihoub, MouadhAbdallah, JadLeger, ThibautJoly, NicolasLiebart, Jean-ClaudeJurkun, Ula V.DNA damage induced by reactive carbonyls (mainly methylglyoxal and glyoxal), called DNA glycation, is quantitatively as important as oxidative damage. DNA glycation is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity. However, in contrast to guanine oxidation repair, how glycated DNA is repaired remains undetermined. Here, we found that the parkinsonism-associated protein DJ-1 and its bacterial homologs Hsp31, YhbO, and YajL could repair methylglyoxal- and glyoxal-glycated nucleotides and nucleic acids. DJ-1–depleted cells displayed increased levels of glycated DNA, DNA strand breaks, and phosphorylated p53. Deglycase-deficient bacterial mutants displayed increased levels of glycated DNA and RNA and exhibited strong mutator phenotypes. Thus, DJ-1 and its prokaryotic homologs constitute a major nucleotide repair system that we name guanine glycation repair.PublishedN/A2019-05-28T10:34:13Z2019-05-28T10:34:13Z20172019-05-28Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article0036-8075http://hdl.handle.net/10725/10677https://doi.org/10.1126/science.aag1095Richarme, G., Liu, C., Mihoub, M., Abdallah, J., Leger, T., Joly, N., ... & Dairou, J. (2017). Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science, 357(6347), 208-211.http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.phphttps://science.sciencemag.org/content/357/6347/208/tab-article-infoenScienceinfo:eu-repo/semantics/openAccessoai:laur.lau.edu.lb:10725/106772021-03-19T10:45:16Z |
| spellingShingle | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs Richarme, Gilbert |
| status_str | publishedVersion |
| title | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs |
| title_full | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs |
| title_fullStr | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs |
| title_full_unstemmed | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs |
| title_short | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs |
| title_sort | Guanine glycation repair by DJ-1/Park7 and its bacterial homologs |
| url | http://hdl.handle.net/10725/10677 https://doi.org/10.1126/science.aag1095 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php https://science.sciencemag.org/content/357/6347/208/tab-article-info |