The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA.
8-oxo-7,8-dihydroadenine (8-oxoAde) is a major product of adenine modification by reactive oxygen species. So far, only one mammalian DNA glycosylase, 8-oxoguanine-DNA-glycosylase 1 (OGG1), has been shown to excise 8-oxoAde, exclusively from pairs with Cyt. We have found that endonuclease VIII-like...
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| Format: | Journal article |
| Language: | English |
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2010
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| _version_ | 1797082822036422656 |
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| author | Grin, I Dianov, G Zharkov, DO |
| author_facet | Grin, I Dianov, G Zharkov, DO |
| author_sort | Grin, I |
| collection | OXFORD |
| description | 8-oxo-7,8-dihydroadenine (8-oxoAde) is a major product of adenine modification by reactive oxygen species. So far, only one mammalian DNA glycosylase, 8-oxoguanine-DNA-glycosylase 1 (OGG1), has been shown to excise 8-oxoAde, exclusively from pairs with Cyt. We have found that endonuclease VIII-like protein 1 (NEIL1), a mammalian homolog of bacterial endonuclease VIII, can efficiently remove 8-oxoAde from 8-oxoAde:Cyt pairs but not from other contexts. In an in vitro reconstituted system, reactions containing OGG1 produced a fully repaired product, whereas NEIL1 caused an abortive initiation of repair, stopping after 8-oxoAde removal and DNA strand cleavage. This block was partially relieved by polynucleotide kinase/3'-phosphatase. Thus, two alternative routes of 8-oxoAde repair may exist in mammals. |
| first_indexed | 2024-03-07T01:33:17Z |
| format | Journal article |
| id | oxford-uuid:944c4f59-e2b9-433a-8c14-c5576c1ac53e |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:33:17Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:944c4f59-e2b9-433a-8c14-c5576c1ac53e2022-03-26T23:38:26ZThe role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:944c4f59-e2b9-433a-8c14-c5576c1ac53eEnglishSymplectic Elements at Oxford2010Grin, IDianov, GZharkov, DO8-oxo-7,8-dihydroadenine (8-oxoAde) is a major product of adenine modification by reactive oxygen species. So far, only one mammalian DNA glycosylase, 8-oxoguanine-DNA-glycosylase 1 (OGG1), has been shown to excise 8-oxoAde, exclusively from pairs with Cyt. We have found that endonuclease VIII-like protein 1 (NEIL1), a mammalian homolog of bacterial endonuclease VIII, can efficiently remove 8-oxoAde from 8-oxoAde:Cyt pairs but not from other contexts. In an in vitro reconstituted system, reactions containing OGG1 produced a fully repaired product, whereas NEIL1 caused an abortive initiation of repair, stopping after 8-oxoAde removal and DNA strand cleavage. This block was partially relieved by polynucleotide kinase/3'-phosphatase. Thus, two alternative routes of 8-oxoAde repair may exist in mammals. |
| spellingShingle | Grin, I Dianov, G Zharkov, DO The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. |
| title | The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. |
| title_full | The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. |
| title_fullStr | The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. |
| title_full_unstemmed | The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. |
| title_short | The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. |
| title_sort | role of mammalian neil1 protein in the repair of 8 oxo 7 8 dihydroadenine in dna |
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