Chloroacetaldehyde-induced mutagenesis in Escherichia coli: the role of AlkB protein in repair of 3,N(4)-ethenocytosine and 3,N(4)-alpha-hydroxyethanocytosine.
Identifieur interne : 002648 ( Main/Exploration ); précédent : 002647; suivant : 002649Chloroacetaldehyde-induced mutagenesis in Escherichia coli: the role of AlkB protein in repair of 3,N(4)-ethenocytosine and 3,N(4)-alpha-hydroxyethanocytosine.
Auteurs : Agnieszka M. Maciejewska [Pologne] ; Karol P. Ruszel ; Jadwiga Nieminuszczy ; Joanna Lewicka ; Beata Sokołowska ; Elzbieta Grzesiuk ; Jarosław T. Ku MierekSource :
- Mutation research [ 0027-5107 ] ; 2010.
Descripteurs français
- KwdFr :
- Acétaldéhyde (analogues et dérivés), Acétaldéhyde (toxicité), Cytosine (analogues et dérivés), Cytosine (métabolisme), Escherichia coli (génétique), Mixed function oxygenases (métabolisme), Mutagenèse, Mutagènes (toxicité), Protéines Escherichia coli (métabolisme), Réparation de l'ADN, Tests de mutagénicité, Transformation bactérienne.
- MESH :
- analogues et dérivés : Acétaldéhyde, Cytosine.
- génétique : Escherichia coli.
- métabolisme : Cytosine, Mixed function oxygenases, Protéines Escherichia coli.
- toxicité : Acétaldéhyde, Mutagènes.
- Mutagenèse, Réparation de l'ADN, Tests de mutagénicité, Transformation bactérienne.
English descriptors
- KwdEn :
- Acetaldehyde (analogs & derivatives), Acetaldehyde (toxicity), Cytosine (analogs & derivatives), Cytosine (metabolism), DNA Repair, Escherichia coli (genetics), Escherichia coli Proteins (metabolism), Mixed Function Oxygenases (metabolism), Mutagenesis, Mutagenicity Tests, Mutagens (toxicity), Transformation, Bacterial.
- MESH :
- chemical , analogs & derivatives : Acetaldehyde, Cytosine.
- chemical , metabolism : Cytosine, Escherichia coli Proteins, Mixed Function Oxygenases.
- chemical , toxicity : Acetaldehyde, Mutagens.
- genetics : Escherichia coli.
- DNA Repair, Mutagenesis, Mutagenicity Tests, Transformation, Bacterial.
Abstract
Etheno (epsilon) adducts are formed in reaction of DNA bases with various environmental carcinogens and endogenously created products of lipid peroxidation. Chloroacetaldehyde (CAA), a metabolite of carcinogen vinyl chloride, is routinely used to generate epsilon-adducts. We studied the role of AlkB, along with AlkA and Mug proteins, all engaged in repair of epsilon-adducts, in CAA-induced mutagenesis. The test system used involved pIF102 and pIF104 plasmids bearing the lactose operon of CC102 or CC104 origin (Cupples and Miller (1989) [17]) which allowed to monitor Lac(+) revertants, the latter arose by GC-->AT or GC-->TA substitutions, respectively, as a result of modification of guanine and cytosine. The plasmids were CAA-damaged in vitro and replicated in Escherichia coli of various genetic backgrounds. To modify the levels of AlkA and AlkB proteins, mutagenesis was studied in E. coli cells induced or not in adaptive response. Formation of varepsilonC proceeds via a relatively stable intermediate, 3,N(4)-alpha-hydroxyethanocytosine (HEC), which allowed to compare repair of both adducts. The results indicate that all three genes, alkA, alkB and microg, are engaged in alleviation of CAA-induced mutagenesis. The frequency of mutation was higher in AlkA-, AlkB- and Mug-deficient strains in comparison to alkA(+), alkB(+), and microg(+) controls. Considering the levels of CAA-induced Lac(+) revertants in strains harboring the pIF plasmids and induced or not in adaptive response, we conclude that AlkB protein is engaged in the repair of epsilonC and HEC in vivo. Using the modified TTCTT 5-mers as substrates, we confirmed in vitro that AlkB protein repairs epsilonC and HEC although far less efficiently than the reference adduct 3-methylcytosine. The pH optimum for repair of HEC and epsilonC is significantly different from that for 3-methylcytosine. We propose that the protonated form of adduct interact in active site of AlkB protein.
DOI: 10.1016/j.mrfmmm.2009.11.005
PubMed: 19941873
Affiliations:
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Le document en format XML
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Maciejewska</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, 5A Pawińskiego Str, Poland.</nlm:affiliation><country xml:lang="fr">Pologne</country><wicri:regionArea>Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, 5A Pawińskiego Str</wicri:regionArea><wicri:noRegion>5A Pawińskiego Str</wicri:noRegion></affiliation></author><author><name sortKey="Ruszel, Karol P" sort="Ruszel, Karol P" uniqKey="Ruszel K" first="Karol P" last="Ruszel">Karol P. Ruszel</name></author><author><name sortKey="Nieminuszczy, Jadwiga" sort="Nieminuszczy, Jadwiga" uniqKey="Nieminuszczy J" first="Jadwiga" last="Nieminuszczy">Jadwiga Nieminuszczy</name></author><author><name sortKey="Lewicka, Joanna" sort="Lewicka, Joanna" uniqKey="Lewicka J" first="Joanna" last="Lewicka">Joanna Lewicka</name></author><author><name sortKey="Sokolowska, Beata" sort="Sokolowska, Beata" uniqKey="Sokolowska B" first="Beata" last="Sokołowska">Beata Sokołowska</name></author><author><name sortKey="Grzesiuk, Elzbieta" sort="Grzesiuk, Elzbieta" uniqKey="Grzesiuk E" first="Elzbieta" last="Grzesiuk">Elzbieta Grzesiuk</name></author><author><name sortKey="Ku Mierek, Jaroslaw T" sort="Ku Mierek, Jaroslaw T" uniqKey="Ku Mierek J" first="Jarosław T" last="Ku Mierek">Jarosław T. Ku Mierek</name></author></analytic><series><title level="j">Mutation research</title><idno type="ISSN">0027-5107</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetaldehyde (analogs & derivatives)</term><term>Acetaldehyde (toxicity)</term><term>Cytosine (analogs & derivatives)</term><term>Cytosine (metabolism)</term><term>DNA Repair</term><term>Escherichia coli (genetics)</term><term>Escherichia coli Proteins (metabolism)</term><term>Mixed Function Oxygenases (metabolism)</term><term>Mutagenesis</term><term>Mutagenicity Tests</term><term>Mutagens (toxicity)</term><term>Transformation, Bacterial</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acétaldéhyde (analogues et dérivés)</term><term>Acétaldéhyde (toxicité)</term><term>Cytosine (analogues et dérivés)</term><term>Cytosine (métabolisme)</term><term>Escherichia coli (génétique)</term><term>Mixed function oxygenases (métabolisme)</term><term>Mutagenèse</term><term>Mutagènes (toxicité)</term><term>Protéines Escherichia coli (métabolisme)</term><term>Réparation de l'ADN</term><term>Tests de mutagénicité</term><term>Transformation bactérienne</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Acetaldehyde</term><term>Cytosine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytosine</term><term>Escherichia coli Proteins</term><term>Mixed Function Oxygenases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Acetaldehyde</term><term>Mutagens</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acétaldéhyde</term><term>Cytosine</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosine</term><term>Mixed function oxygenases</term><term>Protéines Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Acétaldéhyde</term><term>Mutagènes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>DNA Repair</term><term>Mutagenesis</term><term>Mutagenicity Tests</term><term>Transformation, Bacterial</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Mutagenèse</term><term>Réparation de l'ADN</term><term>Tests de mutagénicité</term><term>Transformation bactérienne</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Etheno (epsilon) adducts are formed in reaction of DNA bases with various environmental carcinogens and endogenously created products of lipid peroxidation. Chloroacetaldehyde (CAA), a metabolite of carcinogen vinyl chloride, is routinely used to generate epsilon-adducts. We studied the role of AlkB, along with AlkA and Mug proteins, all engaged in repair of epsilon-adducts, in CAA-induced mutagenesis. The test system used involved pIF102 and pIF104 plasmids bearing the lactose operon of CC102 or CC104 origin (Cupples and Miller (1989) [17]) which allowed to monitor Lac(+) revertants, the latter arose by GC-->AT or GC-->TA substitutions, respectively, as a result of modification of guanine and cytosine. The plasmids were CAA-damaged in vitro and replicated in Escherichia coli of various genetic backgrounds. To modify the levels of AlkA and AlkB proteins, mutagenesis was studied in E. coli cells induced or not in adaptive response. Formation of varepsilonC proceeds via a relatively stable intermediate, 3,N(4)-alpha-hydroxyethanocytosine (HEC), which allowed to compare repair of both adducts. The results indicate that all three genes, alkA, alkB and microg, are engaged in alleviation of CAA-induced mutagenesis. The frequency of mutation was higher in AlkA-, AlkB- and Mug-deficient strains in comparison to alkA(+), alkB(+), and microg(+) controls. Considering the levels of CAA-induced Lac(+) revertants in strains harboring the pIF plasmids and induced or not in adaptive response, we conclude that AlkB protein is engaged in the repair of epsilonC and HEC in vivo. Using the modified TTCTT 5-mers as substrates, we confirmed in vitro that AlkB protein repairs epsilonC and HEC although far less efficiently than the reference adduct 3-methylcytosine. The pH optimum for repair of HEC and epsilonC is significantly different from that for 3-methylcytosine. We propose that the protonated form of adduct interact in active site of AlkB protein.</div></front></TEI><affiliations><list><country><li>Pologne</li></country></list><tree><noCountry><name sortKey="Grzesiuk, Elzbieta" sort="Grzesiuk, Elzbieta" uniqKey="Grzesiuk E" first="Elzbieta" last="Grzesiuk">Elzbieta Grzesiuk</name><name sortKey="Ku Mierek, Jaroslaw T" sort="Ku Mierek, Jaroslaw T" uniqKey="Ku Mierek J" first="Jarosław T" last="Ku Mierek">Jarosław T. Ku Mierek</name><name sortKey="Lewicka, Joanna" sort="Lewicka, Joanna" uniqKey="Lewicka J" first="Joanna" last="Lewicka">Joanna Lewicka</name><name sortKey="Nieminuszczy, Jadwiga" sort="Nieminuszczy, Jadwiga" uniqKey="Nieminuszczy J" first="Jadwiga" last="Nieminuszczy">Jadwiga Nieminuszczy</name><name sortKey="Ruszel, Karol P" sort="Ruszel, Karol P" uniqKey="Ruszel K" first="Karol P" last="Ruszel">Karol P. Ruszel</name><name sortKey="Sokolowska, Beata" sort="Sokolowska, Beata" uniqKey="Sokolowska B" first="Beata" last="Sokołowska">Beata Sokołowska</name></noCountry><country name="Pologne"><noRegion><name sortKey="Maciejewska, Agnieszka M" sort="Maciejewska, Agnieszka M" uniqKey="Maciejewska A" first="Agnieszka M" last="Maciejewska">Agnieszka M. Maciejewska</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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