A Polycomb complex remains bound through DNA replication in the absence of other eukaryotic proteins

Handle URI:
http://hdl.handle.net/10754/325371
Title:
A Polycomb complex remains bound through DNA replication in the absence of other eukaryotic proteins
Authors:
Lengsfeld, Bettina M.; Berry, Kayla N.; Ghosh, Sharmistha; Takahashi, Masateru; Francis, Nicole J.
Abstract:
Propagation of chromatin states through DNA replication is central to epigenetic regulation and can involve recruitment of chromatin proteins to replicating chromatin through interactions with replication fork components. Here we show using a fully reconstituted T7 bacteriophage system that eukaryotic proteins are not required to tether the Polycomb complex PRC1 to templates during DNA replication. Instead, DNA binding by PRC1 can withstand passage of a simple replication fork.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Lengsfeld BM, Berry KN, Ghosh S, Takahashi M, Francis NJ (2012) A Polycomb complex remains bound through DNA replication in the absence of other eukaryotic proteins. Sci Rep 2. doi:10.1038/srep00661.
Publisher:
Nature Publishing Group
Journal:
Scientific Reports
Issue Date:
17-Sep-2012
DOI:
10.1038/srep00661
PubMed ID:
22993687
PubMed Central ID:
PMC3443814
Type:
Article
ISSN:
20452322
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorLengsfeld, Bettina M.en
dc.contributor.authorBerry, Kayla N.en
dc.contributor.authorGhosh, Sharmisthaen
dc.contributor.authorTakahashi, Masateruen
dc.contributor.authorFrancis, Nicole J.en
dc.date.accessioned2014-08-27T09:49:35Z-
dc.date.available2014-08-27T09:49:35Z-
dc.date.issued2012-09-17en
dc.identifier.citationLengsfeld BM, Berry KN, Ghosh S, Takahashi M, Francis NJ (2012) A Polycomb complex remains bound through DNA replication in the absence of other eukaryotic proteins. Sci Rep 2. doi:10.1038/srep00661.en
dc.identifier.issn20452322en
dc.identifier.pmid22993687en
dc.identifier.doi10.1038/srep00661en
dc.identifier.urihttp://hdl.handle.net/10754/325371en
dc.description.abstractPropagation of chromatin states through DNA replication is central to epigenetic regulation and can involve recruitment of chromatin proteins to replicating chromatin through interactions with replication fork components. Here we show using a fully reconstituted T7 bacteriophage system that eukaryotic proteins are not required to tether the Polycomb complex PRC1 to templates during DNA replication. Instead, DNA binding by PRC1 can withstand passage of a simple replication fork.en
dc.language.isoenen
dc.publisherNature Publishing Groupen
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.subjectDNA directed DNA polymeraseen
dc.subjecthelicaseen
dc.subjectpolycomb group proteinen
dc.subjectvirus DNAen
dc.subjectvirus proteinen
dc.subjectbacteriophage T7en
dc.subjectbinding competitionen
dc.subjectchemistryen
dc.subjectDNA replicationen
dc.subjectgeneticsen
dc.subjectplasmiden
dc.subjectprotein bindingen
dc.subjectBacteriophage T7en
dc.subjectBinding, Competitiveen
dc.subjectDNA Helicasesen
dc.subjectDNA Replicationen
dc.subjectDNA, Viralen
dc.subjectDNA-Directed DNA Polymeraseen
dc.subjectPlasmidsen
dc.subjectPolycomb-Group Proteinsen
dc.subjectProtein Bindingen
dc.subjectViral Proteinsen
dc.titleA Polycomb complex remains bound through DNA replication in the absence of other eukaryotic proteinsen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalScientific Reportsen
dc.identifier.pmcidPMC3443814en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDepartment of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, United Statesen
dc.contributor.institutionDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, United Statesen
dc.contributor.institutionPfizer Vaccine Research, 401 N., Middletown Road, Pearl River, NY, 10965, United Statesen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorTakahashi, Masateruen

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