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Article: DNA-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (CAF-1) drives tetrasome assembly in the wake of DNA replication

TitleDNA-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (CAF-1) drives tetrasome assembly in the wake of DNA replication
Authors
Issue Date2017
Citation
eLife, 2017, v. 6, article no. e22799 How to Cite?
AbstractNucleosome assembly in the wake of DNA replication is a key process that regulates cell identity and survival. Chromatin assembly factor 1 (CAF-1) is a H3-H4 histone chaperone that associates with the replisome and orchestrates chromatin assembly following DNA synthesis. Little is known about the mechanism and structure of this key complex. Here we investigate the CAF-1·H3-H4 binding mode and the mechanism of nucleosome assembly. We show that yeast CAF-1 binding to a H3-H4 dimer activates the Cac1 winged helix domain interaction with DNA. This drives the formation of a transient CAF-1·histone·DNA intermediate containing two CAF-1 complexes, each associated with one H3-H4 dimer. Here, the (H3-H4)2 tetramer is formed and deposited onto DNA. Our work elucidates the molecular mechanism for histone deposition by CAF-1, a reaction that has remained elusive for other histone chaperones, and it advances our understanding of how nucleosomes and their epigenetic information are maintained through DNA replication.
Persistent Identifierhttp://hdl.handle.net/10722/314027
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMattiroli, Francesca-
dc.contributor.authorGu, Yajie-
dc.contributor.authorYadav, Tejas-
dc.contributor.authorBalsbaugh, Jeremy L.-
dc.contributor.authorHarris, Michael R.-
dc.contributor.authorFindlay, Eileen S.-
dc.contributor.authorLiu, Yang-
dc.contributor.authorRadebaugh, Catherine A.-
dc.contributor.authorStargell, Laurie A.-
dc.contributor.authorAhn, Natalie G.-
dc.contributor.authorWhitehouse, Iestyn-
dc.contributor.authorLuger, Karolin-
dc.date.accessioned2022-07-11T04:06:09Z-
dc.date.available2022-07-11T04:06:09Z-
dc.date.issued2017-
dc.identifier.citationeLife, 2017, v. 6, article no. e22799-
dc.identifier.urihttp://hdl.handle.net/10722/314027-
dc.description.abstractNucleosome assembly in the wake of DNA replication is a key process that regulates cell identity and survival. Chromatin assembly factor 1 (CAF-1) is a H3-H4 histone chaperone that associates with the replisome and orchestrates chromatin assembly following DNA synthesis. Little is known about the mechanism and structure of this key complex. Here we investigate the CAF-1·H3-H4 binding mode and the mechanism of nucleosome assembly. We show that yeast CAF-1 binding to a H3-H4 dimer activates the Cac1 winged helix domain interaction with DNA. This drives the formation of a transient CAF-1·histone·DNA intermediate containing two CAF-1 complexes, each associated with one H3-H4 dimer. Here, the (H3-H4)2 tetramer is formed and deposited onto DNA. Our work elucidates the molecular mechanism for histone deposition by CAF-1, a reaction that has remained elusive for other histone chaperones, and it advances our understanding of how nucleosomes and their epigenetic information are maintained through DNA replication.-
dc.languageeng-
dc.relation.ispartofeLife-
dc.titleDNA-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (CAF-1) drives tetrasome assembly in the wake of DNA replication-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.7554/eLife.22799-
dc.identifier.pmid28315523-
dc.identifier.scopuseid_2-s2.0-85017642672-
dc.identifier.volume6-
dc.identifier.spagearticle no. e22799-
dc.identifier.epagearticle no. e22799-
dc.identifier.eissn2050-084X-
dc.identifier.isiWOS:000400015700001-

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