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dc.contributor.author
Ziemski, Michal
dc.contributor.author
Jomaa, Ahmad
dc.contributor.author
Mayer, Daniel
dc.contributor.author
Rutz, Sonja
dc.contributor.author
Giese, Christoph
dc.contributor.author
Veprintsev, Dmitry
dc.contributor.author
Weber-Ban, Eilika
dc.date.accessioned
2018-07-13T09:14:33Z
dc.date.available
2018-07-11T03:13:38Z
dc.date.available
2018-07-13T09:14:33Z
dc.date.issued
2018-05
dc.identifier.other
10.7554/eLife.34055
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/274970
dc.identifier.doi
10.3929/ethz-b-000274970
dc.description.abstract
Cdc48 is a AAA+ ATPase that plays an essential role for many cellular processes in eukaryotic cells. An archaeal homologue of this highly conserved enzyme was shown to directly interact with the 20S proteasome. Here, we analyze the occurrence and phylogeny of a Cdc48 homologue in Actinobacteria and assess its cellular function and possible interaction with the bacterial proteasome. Our data demonstrate that Cdc48-like protein of actinobacteria (Cpa) forms hexameric rings and that the oligomeric state correlates directly with the ATPase activity. Furthermore, we show that the assembled Cpa rings can physically interact with the 20S core particle. Comparison of the Mycobacterium smegmatis wild-type with a cpa knockout strain under carbon starvation uncovers significant changes in the levels of around 500 proteins. Pathway mapping of the observed pattern of changes identifies ribosomal proteins as a particular hotspot, pointing amongst others toward a role of Cpa in ribosome adaptation during starvation.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
eLife Sciences Publ.
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
eLife
ethz.journal.volume
7
en_US
ethz.pages.start
e34055
en_US
ethz.size
27 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
The pupylation-dependent and -independent proteasome pathways of mycobacteria
en_US
ethz.identifier.wos
ethz.identifier.scopus
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::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::08811 - Weber-Ban, Eilika (Tit.-Prof.)
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::08811 - Weber-Ban, Eilika (Tit.-Prof.)
ethz.grant.agreementno
163314
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
ethz.date.deposited
2018-07-11T03:14:04Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2018-07-13T09:14:45Z
ethz.rosetta.lastUpdated
2019-02-03T04:50:34Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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