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dc.contributor.authorFoltman, Magdalena
dc.contributor.authorEvrin, Cecile
dc.contributor.authorDe Piccoli, Giacomo
dc.contributor.authorJones, R
dc.contributor.authorEdmondson, R
dc.contributor.authorKatou, Y
dc.contributor.authorNakato, R
dc.contributor.authorShirahige, K
dc.contributor.authorLabib, Karim
dc.date.accessioned2013-05-20T12:49:43Z
dc.date.available2013-05-20T12:49:43Z
dc.date.issued2013-03-28
dc.identifier.citationEukaryotic replisome components cooperate to process histones during chromosome replication. 2013, 3 (3):892-904 Cell Repen_GB
dc.identifier.issn2211-1247
dc.identifier.pmid23499444
dc.identifier.doi10.1016/j.celrep.2013.02.028
dc.identifier.urihttp://hdl.handle.net/10541/292356
dc.description.abstractDNA unwinding at eukaryotic replication forks displaces parental histones, which must be redeposited onto nascent DNA in order to preserve chromatin structure. By screening systematically for replisome components that pick up histones released from chromatin into a yeast cell extract, we found that the Mcm2 helicase subunit binds histones cooperatively with the FACT (facilitiates chromatin transcription) complex, which helps to re-establish chromatin during transcription. FACT does not associate with the Mcm2-7 helicase at replication origins during G1 phase but is subsequently incorporated into the replisome progression complex independently of histone binding and uniquely among histone chaperones. The amino terminal tail of Mcm2 binds histones via a conserved motif that is dispensable for DNA synthesis per se but helps preserve subtelomeric chromatin, retain the 2 micron minichromosome, and support growth in the absence of Ctf18-RFC. Our data indicate that the eukaryotic replication and transcription machineries use analogous assemblies of multiple chaperones to preserve chromatin integrity.
dc.language.isoenen
dc.rightsArchived with thanks to Cell reportsen_GB
dc.titleEukaryotic replisome components cooperate to process histones during chromosome replication.en
dc.typeArticleen
dc.contributor.departmentPaterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK.en_GB
dc.identifier.journalCell Reportsen_GB
html.description.abstractDNA unwinding at eukaryotic replication forks displaces parental histones, which must be redeposited onto nascent DNA in order to preserve chromatin structure. By screening systematically for replisome components that pick up histones released from chromatin into a yeast cell extract, we found that the Mcm2 helicase subunit binds histones cooperatively with the FACT (facilitiates chromatin transcription) complex, which helps to re-establish chromatin during transcription. FACT does not associate with the Mcm2-7 helicase at replication origins during G1 phase but is subsequently incorporated into the replisome progression complex independently of histone binding and uniquely among histone chaperones. The amino terminal tail of Mcm2 binds histones via a conserved motif that is dispensable for DNA synthesis per se but helps preserve subtelomeric chromatin, retain the 2 micron minichromosome, and support growth in the absence of Ctf18-RFC. Our data indicate that the eukaryotic replication and transcription machineries use analogous assemblies of multiple chaperones to preserve chromatin integrity.


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