Human 8-Oxoguanine Glycosylase OGG1 Cleaves Abasic Sites and Covalently Conjugates to 3'-DNA Termini via Cysteine and Histidine Addition
8-Oxoguanine glycosylase 1 (OGG1) repairs the major oxidative DNA damage, 8-oxo-2'-deoxyguanosine. It has been reported that OGG1 incises the most frequently formed DNA lesion, apurinic/apyrimidinic (AP) site, and in the process a stable DNA-OGG1 cross-link is formed. However, the chemical stru...
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| Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2025-01, Vol.26 (2), p.e202400705 |
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| container_title | Chembiochem : a European journal of chemical biology |
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| creator | Bryan, Cameron Yang, Kun |
| description | 8-Oxoguanine glycosylase 1 (OGG1) repairs the major oxidative DNA damage, 8-oxo-2'-deoxyguanosine. It has been reported that OGG1 incises the most frequently formed DNA lesion, apurinic/apyrimidinic (AP) site, and in the process a stable DNA-OGG1 cross-link is formed. However, the chemical structure of the adduct is not characterized. Here, we report that DNA-OGG1 cross-links result from cysteine and histidine addition to incised AP sites at 3'-DNA termini. |
| doi_str_mv | 10.1002/cbic.202400705 |
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Here, we report that DNA-OGG1 cross-links result from cysteine and histidine addition to incised AP sites at 3'-DNA termini.</description><identifier>ISSN: 1439-4227</identifier><identifier>ISSN: 1439-7633</identifier><identifier>EISSN: 1439-7633</identifier><identifier>DOI: 10.1002/cbic.202400705</identifier><identifier>PMID: 39387674</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Cysteine ; Cysteine - chemistry ; Cysteine - metabolism ; Deoxyguanosine ; Deoxyribonucleic acid ; DNA ; DNA - chemistry ; DNA - metabolism ; DNA adducts ; DNA Damage ; DNA Glycosylases - chemistry ; DNA Glycosylases - metabolism ; DNA structure ; Histidine ; Histidine - chemistry ; Histidine - metabolism ; Humans ; OGG1 protein</subject><ispartof>Chembiochem : a European journal of chemical biology, 2025-01, Vol.26 (2), p.e202400705</ispartof><rights>2024 Wiley-VCH GmbH.</rights><rights>2025 Wiley-VCH GmbH</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c248t-688ec9f8a64fa12c8406a0d01e72376f4a860772f53fa79e4830b0365724c45c3</cites><orcidid>0000-0001-5532-8810</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39387674$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bryan, Cameron</creatorcontrib><creatorcontrib>Yang, Kun</creatorcontrib><title>Human 8-Oxoguanine Glycosylase OGG1 Cleaves Abasic Sites and Covalently Conjugates to 3'-DNA Termini via Cysteine and Histidine Addition</title><title>Chembiochem : a European journal of chemical biology</title><addtitle>Chembiochem</addtitle><description>8-Oxoguanine glycosylase 1 (OGG1) repairs the major oxidative DNA damage, 8-oxo-2'-deoxyguanosine. 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It has been reported that OGG1 incises the most frequently formed DNA lesion, apurinic/apyrimidinic (AP) site, and in the process a stable DNA-OGG1 cross-link is formed. However, the chemical structure of the adduct is not characterized. Here, we report that DNA-OGG1 cross-links result from cysteine and histidine addition to incised AP sites at 3'-DNA termini.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>39387674</pmid><doi>10.1002/cbic.202400705</doi><orcidid>https://orcid.org/0000-0001-5532-8810</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1439-4227 |
| ispartof | Chembiochem : a European journal of chemical biology, 2025-01, Vol.26 (2), p.e202400705 |
| issn | 1439-4227 1439-7633 1439-7633 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Cysteine Cysteine - chemistry Cysteine - metabolism Deoxyguanosine Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism DNA adducts DNA Damage DNA Glycosylases - chemistry DNA Glycosylases - metabolism DNA structure Histidine Histidine - chemistry Histidine - metabolism Humans OGG1 protein |
| title | Human 8-Oxoguanine Glycosylase OGG1 Cleaves Abasic Sites and Covalently Conjugates to 3'-DNA Termini via Cysteine and Histidine Addition |
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