7,8-dihydro-8-oxoadenine, a highly mutagenic adduct, is repaired by Escherichia coli and human mismatch-specific uracil/thymine-DNA glycosylases
Identifieur interne : 000334 ( Pmc/Checkpoint ); précédent : 000333; suivant : 0003357,8-dihydro-8-oxoadenine, a highly mutagenic adduct, is repaired by Escherichia coli and human mismatch-specific uracil/thymine-DNA glycosylases
Auteurs : Ibtissam Talhaoui [France] ; Sophie Couvé [France] ; Alexander A. Ishchenko [France] ; Christophe Kunz ; Primo Sch R ; Murat Saparbaev [France]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 2012.
Abstract
Hydroxyl radicals predominantly react with the C8 of purines forming 7,8-dihydro-8-oxoguanine (8oxoG) and 7,8-dihydro-8-oxoadenine (8oxoA) adducts, which are highly mutagenic in mammalian cells. The majority of oxidized DNA bases are removed by DNA glycosylases in the base excision repair pathway. Here, we report for the first time that human thymine-DNA glycosylase (hTDG) and
Url:
DOI: 10.1093/nar/gks1149
PubMed: 23209024
PubMed Central: 3553953
Affiliations:
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<series><title level="j">Nucleic Acids Research</title>
<idno type="ISSN">0305-1048</idno>
<idno type="eISSN">1362-4962</idno>
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<front><div type="abstract" xml:lang="en"><p>Hydroxyl radicals predominantly react with the C<sub>8</sub>
of purines forming 7,8-dihydro-8-oxoguanine (8oxoG) and 7,8-dihydro-8-oxoadenine (8oxoA) adducts, which are highly mutagenic in mammalian cells. The majority of oxidized DNA bases are removed by DNA glycosylases in the base excision repair pathway. Here, we report for the first time that human thymine-DNA glycosylase (hTDG) and <italic>Escherichia coli</italic>
mismatch-specific uracil-DNA glycosylase (MUG) can remove 8oxoA from 8oxoA•T, 8oxoA•G and 8oxoA•C pairs. Comparison of the kinetic parameters of the reaction indicates that full-length hTDG excises 8oxoA, 3,<italic>N</italic>
<sup>4</sup>
-ethenocytosine (εC) and T with similar efficiency (<italic>k</italic>
<sub>max</sub>
= 0.35, 0.36 and 0.16 min<sup>−1</sup>
, respectively) and is more proficient as compared with its bacterial homologue MUG. The N-terminal domain of the hTDG protein is essential for 8oxoA–DNA glycosylase activity, but not for εC repair. Interestingly, the TDG status had little or no effect on the proliferation rate of mouse embryonic fibroblasts after exposure to γ-irradiation. Nevertheless, using whole cell-free extracts from the DNA glycosylase-deficient murine embryonic fibroblasts and <italic>E. coli</italic>
, we demonstrate that the excision of 8oxoA from 8oxoA•T and 8oxoA•G has an absolute requirement for TDG and MUG, respectively. The data establish that MUG and TDG can counteract the genotoxic effects of 8oxoA residues <italic>in vivo</italic>
.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Nucleic Acids Res</journal-id>
<journal-id journal-id-type="iso-abbrev">Nucleic Acids Res</journal-id>
<journal-id journal-id-type="publisher-id">nar</journal-id>
<journal-id journal-id-type="hwp">nar</journal-id>
<journal-title-group><journal-title>Nucleic Acids Research</journal-title>
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<issn pub-type="ppub">0305-1048</issn>
<issn pub-type="epub">1362-4962</issn>
<publisher><publisher-name>Oxford University Press</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">23209024</article-id>
<article-id pub-id-type="pmc">3553953</article-id>
<article-id pub-id-type="doi">10.1093/nar/gks1149</article-id>
<article-id pub-id-type="publisher-id">gks1149</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Genome Integrity, Repair and Replication</subject>
</subj-group>
</article-categories>
<title-group><article-title>7,8-dihydro-8-oxoadenine, a highly mutagenic adduct, is repaired by <italic>Escherichia coli</italic>
and human mismatch-specific uracil/thymine-DNA glycosylases</article-title>
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<xref ref-type="aff" rid="gks1149-AFF1"><sup>1</sup>
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<xref ref-type="aff" rid="gks1149-AFF1"><sup>1</sup>
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<xref ref-type="aff" rid="gks1149-AFF1"><sup>2</sup>
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<xref ref-type="aff" rid="gks1149-AFF1"><sup>1</sup>
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<xref ref-type="aff" rid="gks1149-AFF1"><sup>3</sup>
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<xref ref-type="aff" rid="gks1149-AFF1"><sup>3</sup>
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<xref ref-type="aff" rid="gks1149-AFF1"><sup>1</sup>
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<xref ref-type="corresp" rid="gks1149-COR1">*</xref>
</contrib>
</contrib-group>
<aff id="gks1149-AFF1"><sup>1</sup>
Groupe «Réparation de l’ADN», Université Paris Sud, Laboratoire «Stabilité Génétique et Oncogenèse» CNRS, UMR 8200, Institut de Cancérologie Gustave Roussy, F-94805 Villejuif Cedex,<sup>2</sup>
Génétique Oncologique EPHE, INSERM U753, Institut de cancérologie Gustave Roussy, Villejuif F-94805, France and<sup>3</sup>
Department of Biomedicine, University of Basel, Basel, CH-4058 Switzerland</aff>
<author-notes><corresp id="gks1149-COR1">*To whom correspondence should be addressed. Tel: <phone>+33 1 42 11 54 04</phone>
; Fax: <fax>+33 1 42 11 50 08</fax>
; Email: <email>smurat@igr.fr</email>
</corresp>
<fn><p>The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>1</month>
<year>2013</year>
</pub-date>
<pub-date pub-type="epub"><day>2</day>
<month>12</month>
<year>2012</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>2</day>
<month>12</month>
<year>2012</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
. </pmc-comment>
<volume>41</volume>
<issue>2</issue>
<fpage>912</fpage>
<lpage>923</lpage>
<history><date date-type="received"><day>18</day>
<month>6</month>
<year>2012</year>
</date>
<date date-type="rev-recd"><day>5</day>
<month>10</month>
<year>2012</year>
</date>
<date date-type="accepted"><day>25</day>
<month>10</month>
<year>2012</year>
</date>
</history>
<permissions><copyright-statement>© The Author(s) 2012. Published by Oxford University Press.</copyright-statement>
<copyright-year>2012</copyright-year>
<license license-type="creative-commons" xlink:href="http://creativecommons.org/licenses/by-nc/3.0"><license-p><pmc-comment>CREATIVE COMMONS</pmc-comment>
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/3.0/">http://creativecommons.org/licenses/by-nc/3.0/</ext-link>
), which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com.</license-p>
</license>
</permissions>
<abstract><p>Hydroxyl radicals predominantly react with the C<sub>8</sub>
of purines forming 7,8-dihydro-8-oxoguanine (8oxoG) and 7,8-dihydro-8-oxoadenine (8oxoA) adducts, which are highly mutagenic in mammalian cells. The majority of oxidized DNA bases are removed by DNA glycosylases in the base excision repair pathway. Here, we report for the first time that human thymine-DNA glycosylase (hTDG) and <italic>Escherichia coli</italic>
mismatch-specific uracil-DNA glycosylase (MUG) can remove 8oxoA from 8oxoA•T, 8oxoA•G and 8oxoA•C pairs. Comparison of the kinetic parameters of the reaction indicates that full-length hTDG excises 8oxoA, 3,<italic>N</italic>
<sup>4</sup>
-ethenocytosine (εC) and T with similar efficiency (<italic>k</italic>
<sub>max</sub>
= 0.35, 0.36 and 0.16 min<sup>−1</sup>
, respectively) and is more proficient as compared with its bacterial homologue MUG. The N-terminal domain of the hTDG protein is essential for 8oxoA–DNA glycosylase activity, but not for εC repair. Interestingly, the TDG status had little or no effect on the proliferation rate of mouse embryonic fibroblasts after exposure to γ-irradiation. Nevertheless, using whole cell-free extracts from the DNA glycosylase-deficient murine embryonic fibroblasts and <italic>E. coli</italic>
, we demonstrate that the excision of 8oxoA from 8oxoA•T and 8oxoA•G has an absolute requirement for TDG and MUG, respectively. The data establish that MUG and TDG can counteract the genotoxic effects of 8oxoA residues <italic>in vivo</italic>
.</p>
</abstract>
<counts><page-count count="12"></page-count>
</counts>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>France</li>
</country>
<region><li>Île-de-France</li>
</region>
<settlement><li>Villejuif</li>
</settlement>
<orgName><li>Université Paris-Sud</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Kunz, Christophe" sort="Kunz, Christophe" uniqKey="Kunz C" first="Christophe" last="Kunz">Christophe Kunz</name>
<name sortKey="Sch R, Primo" sort="Sch R, Primo" uniqKey="Sch R P" first="Primo" last="Sch R">Primo Sch R</name>
</noCountry>
<country name="France"><region name="Île-de-France"><name sortKey="Talhaoui, Ibtissam" sort="Talhaoui, Ibtissam" uniqKey="Talhaoui I" first="Ibtissam" last="Talhaoui">Ibtissam Talhaoui</name>
</region>
<name sortKey="Couve, Sophie" sort="Couve, Sophie" uniqKey="Couve S" first="Sophie" last="Couvé">Sophie Couvé</name>
<name sortKey="Couve, Sophie" sort="Couve, Sophie" uniqKey="Couve S" first="Sophie" last="Couvé">Sophie Couvé</name>
<name sortKey="Ishchenko, Alexander A" sort="Ishchenko, Alexander A" uniqKey="Ishchenko A" first="Alexander A." last="Ishchenko">Alexander A. Ishchenko</name>
<name sortKey="Saparbaev, Murat" sort="Saparbaev, Murat" uniqKey="Saparbaev M" first="Murat" last="Saparbaev">Murat Saparbaev</name>
</country>
</tree>
</affiliations>
</record>
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