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dc.contributor.author
Sabath, Kevin
dc.contributor.author
Stäubli, Melanie L.
dc.contributor.author
Marti, Sabrina
dc.contributor.author
Leitner, Alexander
dc.contributor.author
Moes, Murielle
dc.contributor.author
Jonas, Stefanie
dc.date.accessioned
2020-07-30T17:28:54Z
dc.date.available
2020-07-19T02:52:27Z
dc.date.available
2020-07-30T17:28:54Z
dc.date.issued
2020-07-09
dc.identifier.issn
2041-1723
dc.identifier.other
10.1038/s41467-020-17232-2
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/426934
dc.identifier.doi
10.3929/ethz-b-000426934
dc.description.abstract
The Integrator complex processes 3'-ends of spliceosomal small nuclear RNAs (snRNAs). Furthermore, it regulates transcription of protein coding genes by terminating transcription after unstable pausing. The molecular basis for Integrator's functions remains obscure. Here, we show that INTS10, Asunder/INTS13 and INTS14 form a separable, functional Integrator module. The structure of INTS13-INTS14 reveals a strongly entwined complex with a unique chain interlink. Unexpected structural homology to the Ku70-Ku80 DNA repair complex suggests nucleic acid affinity. Indeed, the module displays affinity for DNA and RNA but prefers RNA hairpins. While the module plays an accessory role in snRNA maturation, it has a stronger influence on transcription termination after pausing. Asunder/INTS13 directly binds Integrator's cleavage module via a conserved C-terminal motif that is involved in snRNA processing and required for spermatogenesis. Collectively, our data establish INTS10-INTS13-INTS14 as a nucleic acid-binding module and suggest that it brings cleavage module and target transcripts into proximity.
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.title
INTS10-INTS13-INTS14 form a functional module of Integrator that binds nucleic acids and the cleavage module
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
Nature Communications
ethz.journal.volume
11
en_US
ethz.journal.abbreviated
Nat Commun
ethz.pages.start
3422
en_US
ethz.size
16 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
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::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09609 - Jonas, Stefanie / Jonas, Stefanie
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09609 - Jonas, Stefanie / Jonas, Stefanie
ethz.date.deposited
2020-07-19T02:52:47Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2020-07-30T17:29:09Z
ethz.rosetta.lastUpdated
2021-02-15T15:45:50Z
ethz.rosetta.versionExported
true
ethz.COinS
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