Crosslinking of the NER damage recognition proteins XPC-HR23B, XPA and RPA to photoreactive probes that mimic DNA damages.
Identifieur interne : 002194 ( PubMed/Curation ); précédent : 002193; suivant : 002195Crosslinking of the NER damage recognition proteins XPC-HR23B, XPA and RPA to photoreactive probes that mimic DNA damages.
Auteurs : Ekaterina A. Maltseva [Russie] ; Nadejda I. Rechkunova ; Ludovic C. Gillet ; Irina O. Petruseva ; Orlando D. Sch Rer ; Olga I. LavrikSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2007.
Descripteurs français
- KwdFr :
- Adduits à l'ADN (), Altération de l'ADN, Animaux, Cellules HeLa, Dosage biologique, Escherichia coli (génétique), Histidine (), Humains, Protéine A de réplication (génétique), Protéine A de réplication (isolement et purification), Protéine A de réplication (métabolisme), Protéine XPA (isolement et purification), Protéine XPA (métabolisme), Protéines de liaison à l'ADN (), Protéines de liaison à l'ADN (isolement et purification), Protéines de liaison à l'ADN (métabolisme), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), Rayons ultraviolets, Réactifs réticulants (métabolisme), Sondes d'ADN (effets des radiations), Sondes d'ADN (métabolisme), Spodoptera (cytologie), Spodoptera (métabolisme).
- MESH :
- cytologie : Spodoptera.
- effets des radiations : Sondes d'ADN.
- génétique : Escherichia coli, Protéine A de réplication.
- isolement et purification : Protéine A de réplication, Protéine XPA, Protéines de liaison à l'ADN, Protéines recombinantes.
- métabolisme : Protéine A de réplication, Protéine XPA, Protéines de liaison à l'ADN, Protéines recombinantes, Réactifs réticulants, Sondes d'ADN, Spodoptera.
- Adduits à l'ADN, Altération de l'ADN, Animaux, Cellules HeLa, Dosage biologique, Histidine, Humains, Protéines de liaison à l'ADN, Rayons ultraviolets.
English descriptors
- KwdEn :
- Animals, Biological Assay, Cross-Linking Reagents (metabolism), DNA Adducts (chemistry), DNA Damage, DNA Probes (metabolism), DNA Probes (radiation effects), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (isolation & purification), DNA-Binding Proteins (metabolism), Escherichia coli (genetics), HeLa Cells, Histidine (chemistry), Humans, Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Replication Protein A (genetics), Replication Protein A (isolation & purification), Replication Protein A (metabolism), Spodoptera (cytology), Spodoptera (metabolism), Ultraviolet Rays, Xeroderma Pigmentosum Group A Protein (isolation & purification), Xeroderma Pigmentosum Group A Protein (metabolism).
- MESH :
- chemical , chemistry : DNA Adducts, DNA-Binding Proteins, Histidine.
- chemical , genetics : Replication Protein A.
- chemical , isolation & purification : DNA-Binding Proteins, Recombinant Proteins, Replication Protein A, Xeroderma Pigmentosum Group A Protein.
- chemical , metabolism : Cross-Linking Reagents, DNA Probes, DNA-Binding Proteins, Recombinant Proteins, Replication Protein A, Xeroderma Pigmentosum Group A Protein.
- chemical , radiation effects : DNA Probes.
- cytology : Spodoptera.
- genetics : Escherichia coli.
- metabolism : Spodoptera.
- Animals, Biological Assay, DNA Damage, HeLa Cells, Humans, Ultraviolet Rays.
Abstract
A new assay to probe the mechanism of mammalian nucleotide excision repair (NER) was developed. Photoreactive arylazido analogues of dNMP in DNA were shown to be substrates for the human NER system. Oligonucleotides carrying photoreactive "damages" were prepared using the multi-stage protocol including one-nucleotide gap filling by DNA polymerase beta using photoreactive dCTP or dUTP analogues followed by ligation of the resulting nick. Photoreactive 60-mers were annealed with single-stranded pBluescript II SK (+) and subsequently primer extension reactions were performed. Incubation of HeLa extracts with the plasmids containing photoreactive moieties resulted in an excision pattern typical of NER. DNA duplexes containing photoreactive analogues were used to analyze the interaction of XPC-HR23B, RPA, and XPA with damaged DNA using the photocrosslinking assay. Crosslinking of the XPC-HR23B complex with photoreactive 60-mers resulted in modification of its XPC subunit. RPA crosslinked to ssDNA or mismatched dsDNA more efficiently than to dsDNA, whereas XPA did not show a preference for any of the DNA species. XPC and XPA photocrosslinking to DNA decreased in the presence of Mg(2+) whereas RPA crosslinking to DNA was not sensitive to this cofactor. Our data establish a photocrosslinking assay for the investigation of the damage recognition step in human nucleotide excision repair.
DOI: 10.1016/j.bbagen.2007.01.007
PubMed: 17320292
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pubmed:17320292Le document en format XML
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<term>DNA Damage</term>
<term>DNA Probes (metabolism)</term>
<term>DNA Probes (radiation effects)</term>
<term>DNA-Binding Proteins (chemistry)</term>
<term>DNA-Binding Proteins (isolation & purification)</term>
<term>DNA-Binding Proteins (metabolism)</term>
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<term>HeLa Cells</term>
<term>Histidine (chemistry)</term>
<term>Humans</term>
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<term>Recombinant Proteins (metabolism)</term>
<term>Replication Protein A (genetics)</term>
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<term>Replication Protein A (metabolism)</term>
<term>Spodoptera (cytology)</term>
<term>Spodoptera (metabolism)</term>
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<term>Dosage biologique</term>
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<term>Protéines de liaison à l'ADN</term>
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<term>DNA Damage</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Ultraviolet Rays</term>
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<term>Altération de l'ADN</term>
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<term>Cellules HeLa</term>
<term>Dosage biologique</term>
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<front><div type="abstract" xml:lang="en">A new assay to probe the mechanism of mammalian nucleotide excision repair (NER) was developed. Photoreactive arylazido analogues of dNMP in DNA were shown to be substrates for the human NER system. Oligonucleotides carrying photoreactive "damages" were prepared using the multi-stage protocol including one-nucleotide gap filling by DNA polymerase beta using photoreactive dCTP or dUTP analogues followed by ligation of the resulting nick. Photoreactive 60-mers were annealed with single-stranded pBluescript II SK (+) and subsequently primer extension reactions were performed. Incubation of HeLa extracts with the plasmids containing photoreactive moieties resulted in an excision pattern typical of NER. DNA duplexes containing photoreactive analogues were used to analyze the interaction of XPC-HR23B, RPA, and XPA with damaged DNA using the photocrosslinking assay. Crosslinking of the XPC-HR23B complex with photoreactive 60-mers resulted in modification of its XPC subunit. RPA crosslinked to ssDNA or mismatched dsDNA more efficiently than to dsDNA, whereas XPA did not show a preference for any of the DNA species. XPC and XPA photocrosslinking to DNA decreased in the presence of Mg(2+) whereas RPA crosslinking to DNA was not sensitive to this cofactor. Our data establish a photocrosslinking assay for the investigation of the damage recognition step in human nucleotide excision repair.</div>
</front>
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<Month>05</Month>
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<ArticleTitle>Crosslinking of the NER damage recognition proteins XPC-HR23B, XPA and RPA to photoreactive probes that mimic DNA damages.</ArticleTitle>
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<Abstract><AbstractText>A new assay to probe the mechanism of mammalian nucleotide excision repair (NER) was developed. Photoreactive arylazido analogues of dNMP in DNA were shown to be substrates for the human NER system. Oligonucleotides carrying photoreactive "damages" were prepared using the multi-stage protocol including one-nucleotide gap filling by DNA polymerase beta using photoreactive dCTP or dUTP analogues followed by ligation of the resulting nick. Photoreactive 60-mers were annealed with single-stranded pBluescript II SK (+) and subsequently primer extension reactions were performed. Incubation of HeLa extracts with the plasmids containing photoreactive moieties resulted in an excision pattern typical of NER. DNA duplexes containing photoreactive analogues were used to analyze the interaction of XPC-HR23B, RPA, and XPA with damaged DNA using the photocrosslinking assay. Crosslinking of the XPC-HR23B complex with photoreactive 60-mers resulted in modification of its XPC subunit. RPA crosslinked to ssDNA or mismatched dsDNA more efficiently than to dsDNA, whereas XPA did not show a preference for any of the DNA species. XPC and XPA photocrosslinking to DNA decreased in the presence of Mg(2+) whereas RPA crosslinking to DNA was not sensitive to this cofactor. Our data establish a photocrosslinking assay for the investigation of the damage recognition step in human nucleotide excision repair.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maltseva</LastName>
<ForeName>Ekaterina A</ForeName>
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<ForeName>Nadejda I</ForeName>
<Initials>NI</Initials>
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<Author ValidYN="Y"><LastName>Gillet</LastName>
<ForeName>Ludovic C</ForeName>
<Initials>LC</Initials>
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<Author ValidYN="Y"><LastName>Petruseva</LastName>
<ForeName>Irina O</ForeName>
<Initials>IO</Initials>
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<Author ValidYN="Y"><LastName>Schärer</LastName>
<ForeName>Orlando D</ForeName>
<Initials>OD</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lavrik</LastName>
<ForeName>Olga I</ForeName>
<Initials>OI</Initials>
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<ArticleId IdType="doi">10.1016/j.bbagen.2007.01.007</ArticleId>
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