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dc.contributor.author
Gabizon, Ronen
dc.contributor.author
Brandt, Tobias
dc.contributor.author
Sukenik, Shahar
dc.contributor.author
Lahav, Noa
dc.contributor.author
Lebendiker, Mario
dc.contributor.author
Shalev, Deborah E.
dc.contributor.author
Veprintsev, Dmitry
dc.contributor.author
Friedler, Assaf
dc.date.accessioned
2018-09-20T07:58:25Z
dc.date.available
2017-06-10T02:00:14Z
dc.date.available
2018-09-20T07:58:25Z
dc.date.issued
2012-05-31
dc.identifier.issn
1932-6203
dc.identifier.other
10.1371/journal.pone.0038060
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/50997
dc.identifier.doi
10.3929/ethz-b-000050997
dc.description.abstract
Oligomerization plays a major role in regulating the activity of many proteins, and in modulating their interactions. p53 is a homotetrameric transcription factor that has a pivotal role in tumor suppression. Its tetramerization domain is contained within its C-terminal domain, which is a site for numerous protein-protein interactions. Those can either depend on or regulate p53 oligomerization. Here we screened an array of peptides derived from proteins known to bind the tetrameric p53 C-terminal domain (p53CTD) and identified ten binding peptides. We quantitatively characterized their binding to p53CTD using fluorescence anisotropy. The peptides bound tetrameric p53CTD with micromolar affinities. Despite the high charge of the binding peptides, electrostatics contributed only mildly to the interactions. NMR studies indicated that the peptides bound p53CTD at defined sites. The most significant chemical shift deviations were observed for the peptides WS100B(81–92), which bound directly to the p53 tetramerization domain, and PKCα(281–295), which stabilized p53CTD in circular dichroism thermal denaturation studies. Using analytical ultracentrifugation, we found that several of the peptides bound preferentially to p53 tetramers. Our results indicate that the protein-protein interactions of p53 are dependent on the oligomerization state of p53. We conclude that peptides may be used to regulate the oligomerization of p53.
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/3.0/
dc.title
Specific Recognition of p53 Tetramers by Peptides Derived from p53 Interacting Proteins
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 3.0 Unported
ethz.journal.title
PLoS ONE
ethz.journal.volume
7
en_US
ethz.journal.issue
5
en_US
ethz.journal.abbreviated
PLoS ONE
ethz.pages.start
e38060
en_US
ethz.size
11 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::03866 - Schertler, Gebhard F. / Schertler, Gebhard F.
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::03866 - Schertler, Gebhard F. / Schertler, Gebhard F.
ethz.date.deposited
2017-06-10T02:00:33Z
ethz.source
ECIT
ethz.identifier.importid
imp59364f5f1d60d85602
ethz.ecitpid
pub:83225
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-14T17:49:52Z
ethz.rosetta.lastUpdated
2018-11-08T02:34:51Z
ethz.rosetta.versionExported
true
ethz.COinS
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