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dc.contributor.authorTallis, Michael
dc.contributor.authorMorra, Rosa
dc.contributor.authorBarkauskaite, Eva
dc.contributor.authorAhel, Ivan
dc.date.accessioned2013-12-20T12:05:50Z
dc.date.available2013-12-20T12:05:50Z
dc.date.issued2013-10-27
dc.identifier.citationPoly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response. 2013: Chromosomaen
dc.identifier.issn1432-0886
dc.identifier.pmid24162931
dc.identifier.doi10.1007/s00412-013-0442-9
dc.identifier.urihttp://hdl.handle.net/10541/308840
dc.description.abstractPoly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some PARPs such as PARP1 to broken DNA induces a substantial wave of PARylation, which results in significant re-structuring of the chromatin microenvironment through modification of chromatin-associated proteins and recruitment of chromatin-modifying proteins. Similarly, other DNA damage response proteins are recruited to the damaged sites via PAR-specific binding modules, and in this way, PAR mediates not only local chromatin architecture but also DNA repair. Here, we discuss the expanding role of PAR in the DNA damage response, with particular focus on chromatin regulation.
dc.languageENG
dc.language.isoenen
dc.rightsArchived with thanks to Chromosomaen
dc.titlePoly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response.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.journalChromosomaen
html.description.abstractPoly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some PARPs such as PARP1 to broken DNA induces a substantial wave of PARylation, which results in significant re-structuring of the chromatin microenvironment through modification of chromatin-associated proteins and recruitment of chromatin-modifying proteins. Similarly, other DNA damage response proteins are recruited to the damaged sites via PAR-specific binding modules, and in this way, PAR mediates not only local chromatin architecture but also DNA repair. Here, we discuss the expanding role of PAR in the DNA damage response, with particular focus on chromatin regulation.


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