A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage.
Identifieur interne : 001E47 ( PubMed/Curation ); précédent : 001E46; suivant : 001E48A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage.
Auteurs : Laurent Cappadocia [Canada] ; Jean-Sébastien Parent ; Eric Zampini ; Etienne Lepage ; Jurgen Sygusch ; Normand BrissonSource :
- Nucleic acids research [ 1362-4962 ] ; 2012.
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 Arabidopsis 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.
DOI: 10.1093/nar/gkr740
PubMed: 21911368
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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">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 Arabidopsis 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21911368</PMID><DateCompleted><Year>2012</Year><Month>02</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1362-4962</ISSN><JournalIssue CitedMedium="Internet"><Volume>40</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Nucleic acids research</Title><ISOAbbreviation>Nucleic Acids Res.</ISOAbbreviation></Journal><ArticleTitle>A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage.</ArticleTitle><Pagination><MedlinePgn>258-69</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/nar/gkr740</ELocationID><Abstract><AbstractText>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 Arabidopsis 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cappadocia</LastName><ForeName>Laurent</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Université de Montréal, CP 6128, Station Centre-Ville, Montréal H3C 3J7, Québec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Parent</LastName><ForeName>Jean-Sébastien</ForeName><Initials>JS</Initials></Author><Author ValidYN="Y"><LastName>Zampini</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Lepage</LastName><ForeName>Etienne</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Sygusch</LastName><ForeName>Jurgen</ForeName><Initials>J</Initials></Author><Author 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