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dc.contributor.author
Mugler, Christopher F.
dc.contributor.author
Hondele, Maria
dc.contributor.author
Heinrich, Stephanie
dc.contributor.author
Sachdev, Ruchika
dc.contributor.author
Vallotton, Pascal
dc.contributor.author
Koek, Adriana Y.
dc.contributor.author
Chan, Leon Y.
dc.contributor.author
Weis, Karsten
dc.date.accessioned
2018-09-11T11:52:57Z
dc.date.available
2017-06-12T16:04:45Z
dc.date.available
2018-09-11T11:52:57Z
dc.date.issued
2016-10
dc.identifier.other
10.7554/eLife.18746
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/122727
dc.identifier.doi
10.3929/ethz-b-000122727
dc.description.abstract
Translational repression and mRNA degradation are critical mechanisms of posttranscriptional gene regulation that help cells respond to internal and external cues. In response to certain stress conditions, many mRNA decay factors are enriched in processing bodies (PBs), cellular structures involved in degradation and/or storage of mRNAs. Yet, how cells regulate assembly and disassembly of PBs remains poorly understood. Here, we show that in budding yeast, mutations in the DEAD-box ATPase Dhh1 that prevent ATP hydrolysis, or that affect the interaction between Dhh1 and Not1, the central scaffold of the CCR4-NOT complex and an activator of the Dhh1 ATPase, prevent PB disassembly in vivo. Intriguingly, this process can be recapitulated in vitro, since recombinant Dhh1 and RNA, in the presence of ATP, phase-separate into liquid droplets that rapidly dissolve upon addition of Not1. Our results identify the ATPase activity of Dhh1 as a critical regulator of PB formation.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
eLife Sciences Publications
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
ATPase activity of the DEAD-box protein Dhh1 controls processing body formation
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
eLife
ethz.journal.volume
5
en_US
ethz.pages.start
e18746
en_US
ethz.size
27 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
Structure and Function of the Nuclear Pore Complex
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.identifier.nebis
007613147
ethz.publication.place
Cambridge
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::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::09464 - Weis, Karsten / Weis, Karsten
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::09464 - Weis, Karsten / Weis, Karsten
ethz.grant.agreementno
159731
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
Projektförderung in Biologie und Medizin (Abteilung III)
ethz.date.deposited
2017-06-12T16:06:23Z
ethz.source
ECIT
ethz.identifier.importid
imp593654e024efa41038
ethz.ecitpid
pub:185054
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-12T14:06:49Z
ethz.rosetta.lastUpdated
2018-11-08T01:57:09Z
ethz.rosetta.versionExported
true
ethz.COinS
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