A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage
Identifieur interne : 002487 ( Main/Exploration ); précédent : 002486; suivant : 002488A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage
Auteurs : Laurent Cappadocia ; Jean-Sébastien Parent ; Éric Zampini ; Étienne Lepage ; Jurgen Sygusch ; Normand BrissonSource :
- Nucleic Acids Research [ 0305-1048 ] ; 2011.
Descripteurs français
- KwdFr :
- ADN simple brin (métabolisme), Altération de l'ADN, Arabidopsis (), Arabidopsis (génétique), Ciprofloxacine (toxicité), Lysine (), Microscopie à force atomique, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines d'Arabidopsis (génétique), Protéines de liaison à l'ADN (), Protéines de liaison à l'ADN (génétique), Protéines de liaison à l'ADN (métabolisme), Protéines de liaison à l'ADN (ultrastructure), Protéines végétales (), Protéines végétales (métabolisme), Protéines végétales (ultrastructure), Solanum tuberosum.
- MESH :
- génétique : Arabidopsis, Protéines d'Arabidopsis, Protéines de liaison à l'ADN.
- métabolisme : ADN simple brin, Protéines de liaison à l'ADN, Protéines végétales.
- toxicité : Ciprofloxacine.
- Altération de l'ADN, Arabidopsis, Lysine, Microscopie à force atomique, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines de liaison à l'ADN, Protéines végétales, Solanum tuberosum.
English descriptors
- KwdEn :
- Arabidopsis (drug effects), Arabidopsis (genetics), Arabidopsis Proteins (genetics), Ciprofloxacin (toxicity), DNA Damage, DNA, Single-Stranded (metabolism), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (genetics), DNA-Binding Proteins (metabolism), DNA-Binding Proteins (ultrastructure), Lysine (chemistry), Microscopy, Atomic Force, Models, Molecular, Mutation, Plant Proteins (chemistry), Plant Proteins (metabolism), Plant Proteins (ultrastructure), Protein Multimerization, Solanum tuberosum.
- MESH :
- chemical , chemistry : DNA-Binding Proteins, Lysine, Plant Proteins.
- chemical , genetics : Arabidopsis Proteins, DNA-Binding Proteins.
- drug effects : Arabidopsis.
- genetics : Arabidopsis.
- chemical , metabolism : DNA, Single-Stranded, DNA-Binding Proteins, Plant Proteins.
- chemical , toxicity : Ciprofloxacin.
- chemical , ultrastructure : DNA-Binding Proteins, Plant Proteins.
- DNA Damage, Microscopy, Atomic Force, Models, Molecular, Mutation, Protein Multimerization, Solanum tuberosum.
Abstract
All organisms have evolved specialized DNA repair mechanisms in order to protect their genome against detrimental lesions such as DNA double-strand breaks. In plant organelles, these damages are repaired either through recombination or through a microhomology-mediated break-induced replication pathway. Whirly proteins are modulators of this second pathway in both chloroplasts and mitochondria. In this precise pathway, tetrameric Whirly proteins are believed to bind single-stranded DNA and prevent spurious annealing of resected DNA molecules with other regions in the genome. In this study, we add a new layer of complexity to this model by showing through atomic force microscopy that tetramers of the potato Whirly protein WHY2 further assemble into hexamers of tetramers, or 24-mers, upon binding long DNA molecules. This process depends on tetramer–tetramer interactions mediated by K67, a highly conserved residue among plant Whirly proteins. Mutation of this residue abolishes the formation of 24-mers without affecting the protein structure or the binding to short DNA molecules. Importantly, we show that an
Url:
DOI: 10.1093/nar/gkr740
PubMed: 21911368
PubMed Central: 3245945
Affiliations:
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sortKey="Cappadocia, Laurent" sort="Cappadocia, Laurent" uniqKey="Cappadocia L" first="Laurent" last="Cappadocia">Laurent Cappadocia</name></author><author><name sortKey="Parent, Jean Sebastien" sort="Parent, Jean Sebastien" uniqKey="Parent J" first="Jean-Sébastien" last="Parent">Jean-Sébastien Parent</name></author><author><name sortKey="Zampini, Eric" sort="Zampini, Eric" uniqKey="Zampini E" first="Éric" last="Zampini">Éric Zampini</name></author><author><name sortKey="Lepage, Etienne" sort="Lepage, Etienne" uniqKey="Lepage E" first="Étienne" last="Lepage">Étienne Lepage</name></author><author><name sortKey="Sygusch, Jurgen" sort="Sygusch, Jurgen" uniqKey="Sygusch J" first="Jurgen" last="Sygusch">Jurgen Sygusch</name></author><author><name sortKey="Brisson, Normand" sort="Brisson, Normand" uniqKey="Brisson N" first="Normand" last="Brisson">Normand Brisson</name></author></analytic><series><title level="j">Nucleic Acids Research</title><idno type="ISSN">0305-1048</idno><idno type="eISSN">1362-4962</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (drug effects)</term><term>Arabidopsis (genetics)</term><term>Arabidopsis Proteins (genetics)</term><term>Ciprofloxacin (toxicity)</term><term>DNA Damage</term><term>DNA, Single-Stranded (metabolism)</term><term>DNA-Binding Proteins (chemistry)</term><term>DNA-Binding Proteins (genetics)</term><term>DNA-Binding Proteins (metabolism)</term><term>DNA-Binding Proteins (ultrastructure)</term><term>Lysine (chemistry)</term><term>Microscopy, Atomic Force</term><term>Models, Molecular</term><term>Mutation</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Plant Proteins (ultrastructure)</term><term>Protein Multimerization</term><term>Solanum tuberosum</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN simple brin (métabolisme)</term><term>Altération de l'ADN</term><term>Arabidopsis ()</term><term>Arabidopsis (génétique)</term><term>Ciprofloxacine (toxicité)</term><term>Lysine ()</term><term>Microscopie à force atomique</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutation</term><term>Protéines d'Arabidopsis (génétique)</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>Protéines de liaison à l'ADN (ultrastructure)</term><term>Protéines végétales ()</term><term>Protéines végétales (métabolisme)</term><term>Protéines végétales (ultrastructure)</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA-Binding Proteins</term><term>Lysine</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arabidopsis Proteins</term><term>DNA-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arabidopsis</term><term>Protéines d'Arabidopsis</term><term>Protéines de liaison à l'ADN</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA, Single-Stranded</term><term>DNA-Binding Proteins</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN simple brin</term><term>Protéines de liaison à l'ADN</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Ciprofloxacin</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Ciprofloxacine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>DNA-Binding Proteins</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>DNA Damage</term><term>Microscopy, Atomic Force</term><term>Models, Molecular</term><term>Mutation</term><term>Protein Multimerization</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Altération de l'ADN</term><term>Arabidopsis</term><term>Lysine</term><term>Microscopie à force atomique</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutation</term><term>Protéines de liaison à l'ADN</term><term>Protéines végétales</term><term>Solanum tuberosum</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>All organisms have evolved specialized DNA repair mechanisms in order to protect their genome against detrimental lesions such as DNA double-strand breaks. In plant organelles, these damages are repaired either through recombination or through a microhomology-mediated break-induced replication pathway. Whirly proteins are modulators of this second pathway in both chloroplasts and mitochondria. In this precise pathway, tetrameric Whirly proteins are believed to bind single-stranded DNA and prevent spurious annealing of resected DNA molecules with other regions in the genome. In this study, we add a new layer of complexity to this model by showing through atomic force microscopy that tetramers of the potato Whirly protein WHY2 further assemble into hexamers of tetramers, or 24-mers, upon binding long DNA molecules. This process depends on tetramer–tetramer interactions mediated by K67, a highly conserved residue among plant Whirly proteins. Mutation of this residue abolishes the formation of 24-mers without affecting the protein structure or the binding to short DNA molecules. Importantly, we show that an <italic>Arabidopsis</italic> Whirly protein mutated for this lysine is unable to rescue the sensitivity of a Whirly-less mutant plant to a DNA double-strand break inducing agent.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Puchta, H" uniqKey="Puchta H">H Puchta</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kimura, S" uniqKey="Kimura S">S Kimura</name></author><author><name sortKey="Sakaguchi, K" uniqKey="Sakaguchi K">K Sakaguchi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Nielsen, Bl" uniqKey="Nielsen B">BL Nielsen</name></author><author><name sortKey="Cupp, Jd" uniqKey="Cupp J">JD Cupp</name></author><author><name sortKey="Brammer, J" uniqKey="Brammer J">J Brammer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Marechal, A" uniqKey="Marechal A">A Maréchal</name></author><author><name 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Normand" sort="Brisson, Normand" uniqKey="Brisson N" first="Normand" last="Brisson">Normand Brisson</name><name sortKey="Cappadocia, Laurent" sort="Cappadocia, Laurent" uniqKey="Cappadocia L" first="Laurent" last="Cappadocia">Laurent Cappadocia</name><name sortKey="Lepage, Etienne" sort="Lepage, Etienne" uniqKey="Lepage E" first="Étienne" last="Lepage">Étienne Lepage</name><name sortKey="Parent, Jean Sebastien" sort="Parent, Jean Sebastien" uniqKey="Parent J" first="Jean-Sébastien" last="Parent">Jean-Sébastien Parent</name><name sortKey="Sygusch, Jurgen" sort="Sygusch, Jurgen" uniqKey="Sygusch J" first="Jurgen" last="Sygusch">Jurgen Sygusch</name><name sortKey="Zampini, Eric" sort="Zampini, Eric" uniqKey="Zampini E" first="Éric" last="Zampini">Éric Zampini</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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