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dc.contributor.author
Ziemski, Michal
dc.contributor.author
Leodolter, Julia
dc.contributor.author
Taylor, Gabrielle
dc.contributor.author
Kerschenmeyer, Anne
dc.contributor.author
Weber-Ban, Eilika
dc.date.accessioned
2021-01-08T13:38:29Z
dc.date.available
2020-05-21T02:28:26Z
dc.date.available
2020-05-22T15:01:34Z
dc.date.available
2021-01-08T13:38:29Z
dc.date.issued
2021-01
dc.identifier.issn
1742-464X
dc.identifier.issn
1742-4658
dc.identifier.other
10.1111/febs.15335
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/416173
dc.description.abstract
In Mycobacterium tuberculosis (Mtb), the Clp protease degradation pathway, mediated by the modular ClpCP and ClpXP protease complexes, is essential for growth and presents an attractive drug target. Employing a bacterial adenylate cyclase two‐hybrid (BACTH) screening approach that we adapted to screen the proteome of an Mtb ORF library, we identify protein interaction partners of the ClpC1 chaperone on a genome‐wide level. Our results demonstrate that bipartite type II toxin–antitoxin (TA) systems represent a major substrate class. Out of the 67 type II TA systems known in Mtb, 25 appear as ClpC1 interaction partners in the BACTH screen, including members of the VapBC, MazEF, and ParDE families, as well as a RelBE member that was identified biochemically. We show that antitoxins of the Vap and Rel families are degraded by ClpCP in vitro. We also demonstrate that ClpCP is responsible for mediating the N‐end rule pathway, since the adaptor protein ClpS supports ClpC‐dependent degradation of an N‐end rule model substrate in vitro.
en_US
dc.language.iso
en
en_US
dc.publisher
Wiley
en_US
dc.subject
Clp protease
en_US
dc.subject
ClpC
en_US
dc.subject
ClpS
en_US
dc.subject
Protein degradation
en_US
dc.subject
Toxin-antitoxin system
en_US
dc.title
Genome‐wide interaction screen for Mycobacterium tuberculosis ClpCP protease reveals toxin–antitoxin systems as a major substrate class
en_US
dc.type
Journal Article
dc.date.published
2020-04-17
ethz.journal.title
The FEBS Journal
ethz.journal.volume
288
en_US
ethz.journal.issue
1
en_US
ethz.journal.abbreviated
FEBS j.
ethz.pages.start
111
en_US
ethz.pages.end
126
en_US
ethz.grant
The pupylation-dependent and -independent proteasome pathways of mycobacteria
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Hoboken, NJ
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
Projektförderung in Biologie und Medizin (Abteilung III)
ethz.date.deposited
2020-05-21T02:28:36Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Metadata only
en_US
ethz.rosetta.installDate
2021-01-08T13:38:37Z
ethz.rosetta.lastUpdated
2021-02-15T23:01:51Z
ethz.rosetta.versionExported
true
ethz.COinS
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