MersV1, PubMed, Corpus, bibRecord, 002976

Polymorphism in N-2-acetylaminofluorene induced DNA structure as revealed by DNase I footprinting.

Identifieur interne : 002976 ( PubMed/Corpus ); précédent : 002975; suivant : 002977

Polymorphism in N-2-acetylaminofluorene induced DNA structure as revealed by DNase I footprinting.

Auteurs : X. Veaute ; R P Fuchs

Source :

Nucleic acids research [ 0305-1048 ] ; 1991.

RBID : pubmed:1945836

English descriptors

KwdEn :
- 2-Acetylaminofluorene (chemistry), Base Sequence, DNA (chemistry), DNA Damage, Deoxyribonuclease I (metabolism), Molecular Sequence Data, Mutation, Nucleic Acid Conformation, Polymorphism, Genetic.
MESH :
- chemical , chemistry : 2-Acetylaminofluorene, DNA.
- chemical , metabolism : Deoxyribonuclease I.
- Base Sequence, DNA Damage, Molecular Sequence Data, Mutation, Nucleic Acid Conformation, Polymorphism, Genetic.

Abstract

In this paper, we have constructed double stranded helices (60-mers) containing a single N-2-acetylaminofluorene (-AAF) adduct covalently bound to one of the three guanine residues of the Narl site (G1G2CG3CC). This sequence was identified as a strong frameshift mutation hot spot for many carcinogens that bind to the C8 position of guanine. Using DNase I as a probe for DNA conformation we show i) that the average size of the helix deformation extends over 3 to 5 base pairs in both directions from the adduct site, and ii) that there is a strong polymorphism in the adduct induced DNA conformation. The present study supports the idea that adducts induce specific sequence dependent local conformational changes in DNA that are differentially recognized and processed by the enzymatic machineries that lead to repair or mutagenesis.

DOI: 10.1093/nar/19.20.5603
PubMed: 1945836

Links to Exploration step

pubmed:1945836

Le document en format XML

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<author><name sortKey="Veaute, X" sort="Veaute, X" uniqKey="Veaute X" first="X" last="Veaute">X. Veaute</name>
<affiliation><nlm:affiliation>Institut de Biologie Moléculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France.</nlm:affiliation>
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<author><name sortKey="Fuchs, R P" sort="Fuchs, R P" uniqKey="Fuchs R" first="R P" last="Fuchs">R P Fuchs</name>
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<term>Deoxyribonuclease I (metabolism)</term>
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<front><div type="abstract" xml:lang="en">In this paper, we have constructed double stranded helices (60-mers) containing a single N-2-acetylaminofluorene (-AAF) adduct covalently bound to one of the three guanine residues of the Narl site (G1G2CG3CC). This sequence was identified as a strong frameshift mutation hot spot for many carcinogens that bind to the C8 position of guanine. Using DNase I as a probe for DNA conformation we show i) that the average size of the helix deformation extends over 3 to 5 base pairs in both directions from the adduct site, and ii) that there is a strong polymorphism in the adduct induced DNA conformation. The present study supports the idea that adducts induce specific sequence dependent local conformational changes in DNA that are differentially recognized and processed by the enzymatic machineries that lead to repair or mutagenesis.</div>
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<Title>Nucleic acids research</Title>
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<Abstract><AbstractText>In this paper, we have constructed double stranded helices (60-mers) containing a single N-2-acetylaminofluorene (-AAF) adduct covalently bound to one of the three guanine residues of the Narl site (G1G2CG3CC). This sequence was identified as a strong frameshift mutation hot spot for many carcinogens that bind to the C8 position of guanine. Using DNase I as a probe for DNA conformation we show i) that the average size of the helix deformation extends over 3 to 5 base pairs in both directions from the adduct site, and ii) that there is a strong polymorphism in the adduct induced DNA conformation. The present study supports the idea that adducts induce specific sequence dependent local conformational changes in DNA that are differentially recognized and processed by the enzymatic machineries that lead to repair or mutagenesis.</AbstractText>
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Polymorphism in N-2-acetylaminofluorene induced DNA structure as revealed by DNase I footprinting.

Polymorphism in N-2-acetylaminofluorene induced DNA structure as revealed by DNase I footprinting.

Source :

English descriptors

Abstract

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