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dc.contributor.author
Tariq, Muhammad
dc.contributor.author
Wegrzyn, Renee
dc.contributor.author
Anwar, Saima
dc.contributor.author
Bukau, Bernd
dc.contributor.author
Paro, Renato
dc.date.accessioned
2023-07-05T08:00:57Z
dc.date.available
2017-06-11T04:17:10Z
dc.date.available
2023-07-05T08:00:57Z
dc.date.issued
2013-06-03
dc.identifier.issn
1471-2164
dc.identifier.other
10.1186/1471-2164-14-374
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/79596
dc.identifier.doi
10.3929/ethz-b-000079596
dc.description.abstract
Background: The Drosophila GAGA factor (GAF) participates in nucleosome remodeling to activate genes, acts as an antirepressor and is associated with heterochromatin, contributing to gene repression. GAF functions are intimately associated to chromatin-based epigenetic control, linking basic transcriptional regulation to heritable long-term maintenance of gene expression. These diverse functions require GAF to interact with different partners in different multiprotein complexes. The two isoforms of GAF depict highly conserved glutamine-rich C-terminal domains (Q domain), which have been implicated in complex formation. Results: Here we show that the Q domains exhibit prion-like properties. In an established yeast test system the two GAF Q domains convey prion activities comparable to well known yeast prions. The Q domains stably maintain two distinct conformational states imposing functional constraints on the fused yeast reporter protein. The prion-like phenotype can be reversibly cured in the presence of guanidine HCl or by over-expression of the Hsp104 chaperone protein. Additionally, when fused to GFP, the Q domains form aggregates in yeast cells. Conclusion: We conclude that prion-like behavior of the GAF Q domain suggests that this C-terminal structure may perform stable conformational switches. Such a self-perpetuating change in the conformation could assist GAF executing its diverse epigenetic functions of gene control in Drosophila.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
BioMed Central
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/2.0/
dc.subject
GAGA factor
en_US
dc.subject
Epigenetics
en_US
dc.subject
Prion-like
en_US
dc.subject
Chromatin
en_US
dc.title
Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 2.0 Generic
ethz.journal.title
BMC Genomics
ethz.journal.volume
14
en_US
ethz.journal.abbreviated
BMC Genomics
ethz.pages.start
374
en_US
ethz.size
11 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02060 - Dep. Biosysteme / Dep. of Biosystems Science and Eng.::03748 - Paro, Renato (emeritus) / Paro, Renato (emeritus)
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02060 - Dep. Biosysteme / Dep. of Biosystems Science and Eng.::03748 - Paro, Renato (emeritus) / Paro, Renato (emeritus)
ethz.date.deposited
2017-06-11T04:17:56Z
ethz.source
ECIT
ethz.identifier.importid
imp59365190cc7f046315
ethz.ecitpid
pub:125003
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-26T19:13:17Z
ethz.rosetta.lastUpdated
2024-02-03T01:11:19Z
ethz.rosetta.versionExported
true
ethz.COinS
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