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dc.contributor.author
Delley, Cyrille L.
dc.contributor.author
Läderach, Jürg
dc.contributor.author
Ziemski, Michał
dc.contributor.author
Bolten, Marcel
dc.contributor.author
Böhringer, Daniel
dc.contributor.author
Weber-Ban, Eilika
dc.date.accessioned
2018-11-01T13:49:10Z
dc.date.available
2017-06-11T16:01:24Z
dc.date.available
2018-11-01T13:49:10Z
dc.date.issued
2014-12-03
dc.identifier.issn
1932-6203
dc.identifier.other
10.1371/journal.pone.0114348
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/97771
dc.identifier.doi
10.3929/ethz-b-000097771
dc.description.abstract
The occurrence of the proteasome in bacteria is limited to the phylum of actinobacteria, where it is maintained in parallel to the usual bacterial compartmentalizing proteases. The role it plays in these organisms is still not fully understood, but in the human pathogen Mycobacterium tuberculosis (Mtb) the proteasome supports persistence in the host. In complex with the ring-shaped ATPase Mpa (called ARC in other actinobacteria), the proteasome can degrade proteins that have been post-translationally modified with the prokaryotic ubiquitin-like protein Pup. Unlike for the eukaryotic proteasome core particle, no other bacterial proteasome interactors have been identified to date. Here we describe and characterize a novel bacterial proteasome activator of Mycobacterium tuberculosis we termed Bpa (Rv3780), using a combination of biochemical and biophysical methods. Bpa features a canonical C-terminal proteasome interaction motif referred to as the HbYX motif, and its orthologs are only found in those actinobacteria encoding the proteasomal subunits. Bpa can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome. Using negative-stain electron microscopy, we show that Bpa forms a ring-shaped homooligomer that can bind coaxially to the face of the proteasome cylinder. Interestingly, Bpa can stimulate the proteasomal degradation of the model substrate β-casein, which suggests it could play a role in the removal of non-native or damaged proteins.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Public Library of Science
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Bacterial Proteasome Activator Bpa (Rv3780) Is a Novel Ring-Shaped Interactor of the Mycobacterial Proteasome
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
PLoS ONE
ethz.journal.volume
9
en_US
ethz.journal.issue
12
en_US
ethz.journal.abbreviated
PLoS ONE
ethz.pages.start
e114348
en_US
ethz.size
18 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.nebis
006206116
ethz.publication.place
San Francisco, CA, USA
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.)
en_US
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.date.deposited
2017-06-11T16:02:11Z
ethz.source
ECIT
ethz.identifier.importid
imp593652e6dc3ea65945
ethz.ecitpid
pub:152774
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-12T13:50:48Z
ethz.rosetta.lastUpdated
2018-11-01T13:49:16Z
ethz.rosetta.versionExported
true
ethz.COinS
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