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dc.contributor.authorMehrotra, Pawan Vinoden
dc.contributor.authorAhel, Draganaen
dc.contributor.authorRyan, Den
dc.contributor.authorWeston, Riaen
dc.contributor.authorWiechens, Nen
dc.contributor.authorKraehenbuehl, Rolfen
dc.contributor.authorOwen-Hughes, Ten
dc.contributor.authorAhel, Ivanen
dc.date.accessioned2011-01-24T10:54:53Z
dc.date.available2011-01-24T10:54:53Z
dc.date.issued2011-01-07
dc.identifier.citationDNA Repair Factor APLF Is a Histone Chaperone. 2011, 41 (1):46-55 Mol Cellen
dc.identifier.issn1097-4164
dc.identifier.pmid21211722
dc.identifier.doi10.1016/j.molcel.2010.12.008
dc.identifier.urihttp://hdl.handle.net/10541/120249
dc.description.abstractPoly(ADP-ribosyl)ation plays a major role in DNA repair, where it regulates chromatin relaxation as one of the critical events in the repair process. However, the molecular mechanism by which poly(ADP-ribose) modulates chromatin remains poorly understood. Here we identify the poly(ADP-ribose)-regulated protein APLF as a DNA-damage-specific histone chaperone. APLF preferentially binds to the histone H3/H4 tetramer via its C-terminal acidic motif, which is homologous to the motif conserved in the histone chaperones of the NAP1L family (NAP1L motif). We further demonstrate that APLF exhibits histone chaperone activities in a manner that is dependent on its acidic domain and that the NAP1L motif is critical for the repair capacity of APLF in vivo. Finally, we identify structural analogs of APLF in lower eukaryotes with the ability to bind histones and localize to the sites of DNA-damage-induced poly(ADP-ribosyl)ation. Collectively, these findings define the involvement of histone chaperones in poly(ADP-ribose)-regulated DNA repair reactions.
dc.language.isoenen
dc.subjectDNA Repairen
dc.titleDNA Repair Factor APLF Is a Histone Chaperone.en
dc.typeArticleen
dc.contributor.departmentCancer Research UK, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK.en
dc.identifier.journalMolecular Cellen
html.description.abstractPoly(ADP-ribosyl)ation plays a major role in DNA repair, where it regulates chromatin relaxation as one of the critical events in the repair process. However, the molecular mechanism by which poly(ADP-ribose) modulates chromatin remains poorly understood. Here we identify the poly(ADP-ribose)-regulated protein APLF as a DNA-damage-specific histone chaperone. APLF preferentially binds to the histone H3/H4 tetramer via its C-terminal acidic motif, which is homologous to the motif conserved in the histone chaperones of the NAP1L family (NAP1L motif). We further demonstrate that APLF exhibits histone chaperone activities in a manner that is dependent on its acidic domain and that the NAP1L motif is critical for the repair capacity of APLF in vivo. Finally, we identify structural analogs of APLF in lower eukaryotes with the ability to bind histones and localize to the sites of DNA-damage-induced poly(ADP-ribosyl)ation. Collectively, these findings define the involvement of histone chaperones in poly(ADP-ribose)-regulated DNA repair reactions.


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