Single-molecule analysis reveals human UV-damaged DNA-binding protein (UV-DDB) dimerizes on DNA via multiple kinetic intermediates
Identifieur interne : 001300 ( Main/Exploration ); précédent : 001299; suivant : 001301Single-molecule analysis reveals human UV-damaged DNA-binding protein (UV-DDB) dimerizes on DNA via multiple kinetic intermediates
Auteurs : Harshad Ghodke [États-Unis] ; Hong Wang [États-Unis] ; Ching L. Hsieh [États-Unis] ; Selamawit Woldemeskel ; Simon C. Watkins [États-Unis] ; Vesna Rapi Otrin [États-Unis] ; Bennett Van Houten [États-Unis]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2014.
Descripteurs français
- KwdFr :
- ADN (), ADN (effets des radiations), ADN (métabolisme), Altération de l'ADN, Boîtes quantiques, Cinétique, Concentration osmolaire, Conformation d'acide nucléique, Conformation des protéines, Dimères de pyrimidine (effets des radiations), Dimères de pyrimidine (métabolisme), Humains, Microscopie de fluorescence, Modèles moléculaires, Multimérisation de protéines, Mutagenèse dirigée, Protéines de liaison à l'ADN (), Protéines de liaison à l'ADN (génétique), Protéines de liaison à l'ADN (métabolisme), Rayons ultraviolets (effets indésirables), Substitution d'acide aminé, Xeroderma pigmentosum (génétique), Xeroderma pigmentosum (métabolisme).
- MESH :
- effets des radiations : ADN, Dimères de pyrimidine.
- effets indésirables : Rayons ultraviolets.
- génétique : Protéines de liaison à l'ADN, Xeroderma pigmentosum.
- métabolisme : ADN, Dimères de pyrimidine, Protéines de liaison à l'ADN, Xeroderma pigmentosum.
- ADN, Altération de l'ADN, Boîtes quantiques, Cinétique, Concentration osmolaire, Conformation d'acide nucléique, Conformation des protéines, Humains, Microscopie de fluorescence, Modèles moléculaires, Multimérisation de protéines, Mutagenèse dirigée, Protéines de liaison à l'ADN, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution, DNA (chemistry), DNA (metabolism), DNA (radiation effects), DNA Damage, DNA-Binding Proteins (chemistry), DNA-Binding Proteins (genetics), DNA-Binding Proteins (metabolism), Humans, Kinetics, Microscopy, Fluorescence, Models, Molecular, Mutagenesis, Site-Directed, Nucleic Acid Conformation, Osmolar Concentration, Protein Conformation, Protein Multimerization, Pyrimidine Dimers (metabolism), Pyrimidine Dimers (radiation effects), Quantum Dots, Ultraviolet Rays (adverse effects), Xeroderma Pigmentosum (genetics), Xeroderma Pigmentosum (metabolism).
- MESH :
- chemical , chemistry : DNA, DNA-Binding Proteins.
- chemical , genetics : DNA-Binding Proteins.
- chemical , metabolism : DNA, DNA-Binding Proteins, Pyrimidine Dimers.
- chemical , radiation effects : DNA, Pyrimidine Dimers.
- adverse effects : Ultraviolet Rays.
- genetics : Xeroderma Pigmentosum.
- metabolism : Xeroderma Pigmentosum.
- Amino Acid Substitution, DNA Damage, Humans, Kinetics, Microscopy, Fluorescence, Models, Molecular, Mutagenesis, Site-Directed, Nucleic Acid Conformation, Osmolar Concentration, Protein Conformation, Protein Multimerization, Quantum Dots.
Abstract
UV damage in genomic DNA is identified by the human UV-damaged DNA-binding protein (UV-DDB). Recognition of DNA damage by UV-DDB serves to initiate global genomic nucleotide excision repair (NER) in humans. Recent work has revealed that UV-DDB dimerizes at sites of damage. This study demonstrates that prior to stable damage recognition, UV-DDB interrogates DNA for damage via a 3D diffusion mechanism coupled to the formation of multiple transient intermediates. Stable binding at sites of damage is achieved by dimerization of UV-DDB. This study also analyzed a disease-causing mutant of UV-DDB, which was found to slide on DNA, while retaining the ability to dimerize on DNA. These results enhance our understanding of damage recognition in NER in humans.
Url:
DOI: 10.1073/pnas.1323856111
PubMed: 24760829
PubMed Central: 4020048
Affiliations:
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Le document en format XML
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Watkins</name><affiliation wicri:level="2"><nlm:aff id="aff5">Center for Biologic Imaging,<institution>University of Pittsburgh School of Medicine</institution>, Pittsburgh, PA 15261</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Rapi Otrin, Vesna" sort="Rapi Otrin, Vesna" uniqKey="Rapi Otrin V" first="Vesna" last="Rapi Otrin">Vesna Rapi Otrin</name><affiliation wicri:level="2"><nlm:aff id="aff2"><institution>University of Pittsburgh Cancer Institute</institution>, Pittsburgh, PA 15213;</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>, Pittsburgh</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff wicri:cut="; and" id="aff4">Department of Microbiology and Molecular Genetics,<institution>University of Pittsburgh School of Medicine</institution>, Pittsburgh, PA 15213</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Van Houten, Bennett" sort="Van Houten, Bennett" uniqKey="Van Houten B" first="Bennett" last="Van Houten">Bennett Van Houten</name><affiliation><nlm:aff id="aff1">Department of Pharmacology and Chemical Biology,<institution>University of Pittsburgh School of Medicine</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation><affiliation wicri:level="2"><nlm:aff id="aff2"><institution>University of Pittsburgh Cancer Institute</institution>, Pittsburgh, PA 15213;</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>, Pittsburgh</wicri:cityArea></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>DNA (chemistry)</term><term>DNA (metabolism)</term><term>DNA (radiation effects)</term><term>DNA Damage</term><term>DNA-Binding Proteins (chemistry)</term><term>DNA-Binding Proteins (genetics)</term><term>DNA-Binding Proteins (metabolism)</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Fluorescence</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Nucleic Acid Conformation</term><term>Osmolar Concentration</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Pyrimidine Dimers (metabolism)</term><term>Pyrimidine Dimers (radiation effects)</term><term>Quantum Dots</term><term>Ultraviolet Rays (adverse effects)</term><term>Xeroderma Pigmentosum (genetics)</term><term>Xeroderma Pigmentosum (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN ()</term><term>ADN (effets des radiations)</term><term>ADN (métabolisme)</term><term>Altération de l'ADN</term><term>Boîtes quantiques</term><term>Cinétique</term><term>Concentration osmolaire</term><term>Conformation d'acide nucléique</term><term>Conformation des protéines</term><term>Dimères de pyrimidine (effets des radiations)</term><term>Dimères de pyrimidine (métabolisme)</term><term>Humains</term><term>Microscopie de fluorescence</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutagenèse dirigée</term><term>Protéines de liaison à l'ADN ()</term><term>Protéines de liaison à l'ADN (génétique)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Rayons ultraviolets (effets indésirables)</term><term>Substitution d'acide aminé</term><term>Xeroderma pigmentosum (génétique)</term><term>Xeroderma pigmentosum (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA</term><term>DNA-Binding Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA-Binding Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA</term><term>DNA-Binding Proteins</term><term>Pyrimidine Dimers</term></keywords><keywords scheme="MESH" type="chemical" qualifier="radiation effects" xml:lang="en"><term>DNA</term><term>Pyrimidine Dimers</term></keywords><keywords scheme="MESH" qualifier="adverse effects" xml:lang="en"><term>Ultraviolet Rays</term></keywords><keywords scheme="MESH" qualifier="effets des radiations" xml:lang="fr"><term>ADN</term><term>Dimères de pyrimidine</term></keywords><keywords scheme="MESH" qualifier="effets indésirables" xml:lang="fr"><term>Rayons ultraviolets</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Xeroderma Pigmentosum</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de liaison à l'ADN</term><term>Xeroderma pigmentosum</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Xeroderma Pigmentosum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN</term><term>Dimères de pyrimidine</term><term>Protéines de liaison à l'ADN</term><term>Xeroderma pigmentosum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>DNA Damage</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Fluorescence</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Nucleic Acid Conformation</term><term>Osmolar Concentration</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Quantum Dots</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN</term><term>Altération de l'ADN</term><term>Boîtes quantiques</term><term>Cinétique</term><term>Concentration osmolaire</term><term>Conformation d'acide nucléique</term><term>Conformation des protéines</term><term>Humains</term><term>Microscopie de fluorescence</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutagenèse dirigée</term><term>Protéines de liaison à l'ADN</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Significance</title><p>UV damage in genomic DNA is identified by the human UV-damaged DNA-binding protein (UV-DDB). Recognition of DNA damage by UV-DDB serves to initiate global genomic nucleotide excision repair (NER) in humans. Recent work has revealed that UV-DDB dimerizes at sites of damage. This study demonstrates that prior to stable damage recognition, UV-DDB interrogates DNA for damage via a 3D diffusion mechanism coupled to the formation of multiple transient intermediates. Stable binding at sites of damage is achieved by dimerization of UV-DDB. This study also analyzed a disease-causing mutant of UV-DDB, which was found to slide on DNA, while retaining the ability to dimerize on DNA. These results enhance our understanding of damage recognition in NER in humans.</p></div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li><li>Pennsylvanie</li></region></list><tree><noCountry><name sortKey="Woldemeskel, Selamawit" sort="Woldemeskel, Selamawit" uniqKey="Woldemeskel S" first="Selamawit" last="Woldemeskel">Selamawit Woldemeskel</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Ghodke, Harshad" sort="Ghodke, Harshad" uniqKey="Ghodke H" first="Harshad" last="Ghodke">Harshad Ghodke</name></region><name sortKey="Hsieh, Ching L" sort="Hsieh, Ching L" uniqKey="Hsieh C" first="Ching L." last="Hsieh">Ching L. Hsieh</name><name sortKey="Hsieh, Ching L" sort="Hsieh, Ching L" uniqKey="Hsieh C" first="Ching L." last="Hsieh">Ching L. Hsieh</name><name sortKey="Rapi Otrin, Vesna" sort="Rapi Otrin, Vesna" uniqKey="Rapi Otrin V" first="Vesna" last="Rapi Otrin">Vesna Rapi Otrin</name><name sortKey="Rapi Otrin, Vesna" sort="Rapi Otrin, Vesna" uniqKey="Rapi Otrin V" first="Vesna" last="Rapi Otrin">Vesna Rapi Otrin</name><name sortKey="Van Houten, Bennett" sort="Van Houten, Bennett" uniqKey="Van Houten B" first="Bennett" last="Van Houten">Bennett Van Houten</name><name sortKey="Wang, Hong" sort="Wang, Hong" uniqKey="Wang H" first="Hong" last="Wang">Hong Wang</name><name sortKey="Watkins, Simon C" sort="Watkins, Simon C" uniqKey="Watkins S" first="Simon C." last="Watkins">Simon C. Watkins</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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