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dc.contributor.author
Kaustov, Lilia
dc.contributor.author
Lemak, Alexander
dc.contributor.author
Wu, Hong
dc.contributor.author
Faini, Marco
dc.contributor.author
Fan, Lixin
dc.contributor.author
Fang, Xianyang
dc.contributor.author
Zeng, Hong
dc.contributor.author
Duan, Shili
dc.contributor.author
Allali-Hassani, Abdellah
dc.contributor.author
Li, Fengling
dc.contributor.author
Wei, Yong
dc.contributor.author
Vedadi, Masoud
dc.contributor.author
Aebersold, Ruedi
dc.contributor.author
Wang, Yunxing
dc.contributor.author
Houliston, Scott
dc.contributor.author
Arrowsmith, Cheryl H.
dc.date.accessioned
2019-09-30T07:24:41Z
dc.date.available
2019-09-29T02:39:01Z
dc.date.available
2019-09-30T07:24:41Z
dc.date.issued
2019-09-26
dc.identifier.issn
1362-4962
dc.identifier.issn
0301-5610
dc.identifier.other
10.1093/nar/gkz697
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/367088
dc.identifier.doi
10.3929/ethz-b-000367088
dc.description.abstract
Histone H3K4 methylation is an epigenetic mark associated with actively transcribed genes. This modification is catalyzed by the mixed lineage leukaemia (MLL) family of histone methyltransferases including MLL1, MLL2, MLL3, MLL4, SET1A and SET1B. The catalytic activity of this family is dependent on interactions with additional conserved proteins, but the structural basis for subunit assembly and the mechanism of regulation is not well understood. We used a hybrid methods approach to study the assembly and biochemical function of the minimally active MLL1 complex (MLL1, WDR5 and RbBP5). A combination of small angle X-ray scattering, cross-linking mass spectrometry, nuclear magnetic resonance spectroscopy and computational modeling were used to generate a dynamic ensemble model in which subunits are assembled via multiple weak interaction sites. We identified a new interaction site between the MLL1 SET domain and the WD40 β-propeller domain of RbBP5, and demonstrate the susceptibility of the catalytic function of the complex to disruption of individual interaction sites.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Oxford University Press
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
The MLL1 trimeric catalytic complex is a dynamic conformational ensemble stabilized by multiple weak interactions
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2019-08-10
ethz.journal.title
Nucleic Acids Research
ethz.journal.volume
47
en_US
ethz.journal.issue
17
en_US
ethz.journal.abbreviated
Nucleic Acids Res.
ethz.pages.start
9433
en_US
ethz.pages.end
9447
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Oxford
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)
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
2019-09-29T02:39:20Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2019-09-30T07:25:01Z
ethz.rosetta.lastUpdated
2022-03-28T23:43:45Z
ethz.rosetta.versionExported
true
ethz.COinS
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