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dc.contributor.author
Kim, Daegeun
dc.contributor.author
Setiaputra, Dheva
dc.contributor.author
Jung, Taeyang
dc.contributor.author
Chung, Jaehee
dc.contributor.author
Leitner, Alexander
dc.contributor.author
Yoon, Jungmin
dc.contributor.author
Aebersold, Ruedi
dc.contributor.author
Hebert, Hans
dc.contributor.author
Yip, Calvin K.
dc.contributor.author
Song, Ji-Joon
dc.date.accessioned
2018-10-24T08:03:54Z
dc.date.available
2017-06-12T07:16:56Z
dc.date.available
2018-10-24T08:03:54Z
dc.date.issued
2016-05-25
dc.identifier.issn
2045-2322
dc.identifier.other
10.1038/srep26702
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/117252
dc.identifier.doi
10.3929/ethz-b-000117252
dc.description.abstract
Chromatin Assembly Complex 1 (CAF-1) is a major histone chaperone involved in deposition of histone H3 and H4 into nucleosome. CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features of the full CAF-1 in complex with histones and other chaperones have not been well characterized. Here, we dissect molecular architecture of yeast CAF-1 (yCAF-1) by cross-linking mass spectrometry (XL-MS) and negative stain single-particle electron microscopy (EM). Our work revealed that Cac1, the largest subunit of yCAF-1, might serve as a major histone binding platform linking Cac2 and Cac3. In addition, EM analysis showed that yCAF-1 adopts a bilobal shape and Cac1 connecting Cac2 and Cac3 to generate a platform for binding histones. This study provides the first structural glimpse of the full CAF-1 complex and a structural framework to understand histone chaperoning processes.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Epigenetics
en_US
dc.subject
Structural biology
en_US
dc.title
Molecular Architecture of Yeast Chromatin Assembly Factor 1
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
Scientific Reports
ethz.journal.volume
6
en_US
ethz.journal.abbreviated
Sci Rep
ethz.pages.start
26702
en_US
ethz.size
7 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.identifier.nebis
006751867
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02538 - Institut für Molekulare Systembiologie / Institute for Molecular Systems Biology::03663 - Aebersold, Rudolf (emeritus) / Aebersold, Rudolf (emeritus)
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02538 - Institut für Molekulare Systembiologie / Institute for Molecular Systems Biology::03663 - Aebersold, Rudolf (emeritus) / Aebersold, Rudolf (emeritus)
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02538 - Institut für Molekulare Systembiologie / Institute for Molecular Systems Biology::03663 - Aebersold, Rudolf (emeritus) / Aebersold, Rudolf (emeritus)
ethz.date.deposited
2017-06-12T07:22:15Z
ethz.source
ECIT
ethz.identifier.importid
imp593654752673d68403
ethz.ecitpid
pub:179153
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-15T09:44:03Z
ethz.rosetta.lastUpdated
2021-02-15T02:16:33Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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