Integrating multi-scale data on homologous recombination into a new recognition mechanism based on simulations of the RecA-ssDNA/dsDNA structure
Identifieur interne : 000795 ( Main/Exploration ); précédent : 000794; suivant : 000796Integrating multi-scale data on homologous recombination into a new recognition mechanism based on simulations of the RecA-ssDNA/dsDNA structure
Auteurs : Darren Yang [États-Unis] ; Benjamin Boyer [France] ; Chantal Prévost [France] ; Claudia Danilowicz [États-Unis] ; Mara Prentiss [États-Unis]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 2015.
Abstract
RecA protein is the prototypical recombinase. Members of the recombinase family can accurately repair double strand breaks in DNA. They also provide crucial links between pairs of sister chromatids in eukaryotic meiosis. A very broad outline of how these proteins align homologous sequences and promote DNA strand exchange has long been known, as are the crystal structures of the RecA-DNA pre- and postsynaptic complexes; however, little is known about the homology searching conformations and the details of how DNA in bacterial genomes is rapidly searched until homologous alignment is achieved. By integrating a physical model of recognition to new modeling work based on docking exploration and molecular dynamics simulation, we present a detailed structure/function model of homology recognition that reconciles extremely quick searching with the efficient and stringent formation of stable strand exchange products and which is consistent with a vast body of previously unexplained experimental results.
Url:
DOI: 10.1093/nar/gkv883
PubMed: 26384422
PubMed Central: 4666392
Affiliations:
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type="main">Integrating multi-scale data on homologous recombination into a new recognition mechanism based on simulations of the RecA-ssDNA/dsDNA structure</title><author><name sortKey="Yang, Darren" sort="Yang, Darren" uniqKey="Yang D" first="Darren" last="Yang">Darren Yang</name><affiliation wicri:level="4"><nlm:aff id="AFF1">School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName><orgName type="university">Université Harvard</orgName></affiliation></author><author><name sortKey="Boyer, Benjamin" sort="Boyer, Benjamin" uniqKey="Boyer B" first="Benjamin" last="Boyer">Benjamin Boyer</name><affiliation wicri:level="1"><nlm:aff id="AFF2">Laboratoire de Biochimie Théorique, CNRS UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, IBPC, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biochimie Théorique, CNRS UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, IBPC, Paris</wicri:regionArea><placeName><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Prevost, Chantal" sort="Prevost, Chantal" uniqKey="Prevost C" first="Chantal" last="Prévost">Chantal Prévost</name><affiliation wicri:level="1"><nlm:aff id="AFF2">Laboratoire de Biochimie Théorique, CNRS UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, IBPC, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biochimie Théorique, CNRS UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, IBPC, Paris</wicri:regionArea><placeName><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Danilowicz, Claudia" sort="Danilowicz, Claudia" uniqKey="Danilowicz C" first="Claudia" last="Danilowicz">Claudia Danilowicz</name><affiliation wicri:level="4"><nlm:aff id="AFF3">Department of Physics, Harvard University, Cambridge, MA 02138, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, Harvard University, Cambridge, MA 02138</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName><orgName type="university">Université Harvard</orgName></affiliation></author><author><name sortKey="Prentiss, Mara" sort="Prentiss, Mara" uniqKey="Prentiss M" first="Mara" last="Prentiss">Mara Prentiss</name><affiliation wicri:level="4"><nlm:aff id="AFF3">Department of Physics, Harvard University, Cambridge, MA 02138, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, Harvard University, Cambridge, MA 02138</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName><orgName type="university">Université Harvard</orgName></affiliation></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="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>RecA protein is the prototypical recombinase. Members of the recombinase family can accurately repair double strand breaks in DNA. They also provide crucial links between pairs of sister chromatids in eukaryotic meiosis. A very broad outline of how these proteins align homologous sequences and promote DNA strand exchange has long been known, as are the crystal structures of the RecA-DNA pre- and postsynaptic complexes; however, little is known about the homology searching conformations and the details of how DNA in bacterial genomes is rapidly searched until homologous alignment is achieved. By integrating a physical model of recognition to new modeling work based on docking exploration and molecular dynamics simulation, we present a detailed structure/function model of homology recognition that reconciles extremely quick searching with the efficient and stringent formation of stable strand exchange products and which is consistent with a vast body of previously unexplained experimental results.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Howard Flanders, P" uniqKey="Howard Flanders P">P. Howard-Flanders</name></author><author><name sortKey="West, S C" uniqKey="West S">S.C. West</name></author><author><name sortKey="Stasiak, A" uniqKey="Stasiak A">A. Stasiak</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Roca, A I" uniqKey="Roca A">A.I. Roca</name></author><author><name sortKey="Cox, M M" uniqKey="Cox M">M.M. 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Kowalczykowski</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Humphrey, W" uniqKey="Humphrey W">W. Humphrey</name></author><author><name sortKey="Dalke, A" uniqKey="Dalke A">A. Dalke</name></author><author><name sortKey="Schulten, K" uniqKey="Schulten K">K. Schulten</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>France</li><li>États-Unis</li></country><region><li>Massachusetts</li></region><settlement><li>Paris</li></settlement><orgName><li>Université Harvard</li></orgName></list><tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Yang, Darren" sort="Yang, Darren" uniqKey="Yang D" first="Darren" last="Yang">Darren Yang</name></region><name sortKey="Danilowicz, Claudia" sort="Danilowicz, Claudia" uniqKey="Danilowicz C" first="Claudia" last="Danilowicz">Claudia Danilowicz</name><name sortKey="Prentiss, Mara" sort="Prentiss, Mara" uniqKey="Prentiss M" first="Mara" last="Prentiss">Mara Prentiss</name></country><country name="France"><noRegion><name sortKey="Boyer, Benjamin" sort="Boyer, Benjamin" uniqKey="Boyer B" first="Benjamin" last="Boyer">Benjamin Boyer</name></noRegion><name sortKey="Prevost, Chantal" sort="Prevost, Chantal" uniqKey="Prevost C" first="Chantal" last="Prévost">Chantal Prévost</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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