Molecular mechanisms of Evening Complex activity in Arabidopsis
dc.contributor.author
Silva, Catarina S.
dc.contributor.author
Nayak, Aditya
dc.contributor.author
Lai, Xuelei
dc.contributor.author
Hutin, Stephanie
dc.contributor.author
Hugouvieux, Véronique
dc.contributor.author
Jung, Jae-Hoon
dc.contributor.author
López-Vidriero, Irene
dc.contributor.author
Franco-Zorrilla, Jose M.
dc.contributor.author
Panigrahi, Kishore C.S.
dc.contributor.author
Nanao, Max H.
dc.contributor.author
Wigge, Philip A.
dc.contributor.author
Zubieta, Chloe
dc.date.accessioned
2020-04-02T09:52:51Z
dc.date.available
2020-04-01T01:33:11Z
dc.date.available
2020-04-02T09:52:51Z
dc.date.issued
2020-03-24
dc.identifier.issn
0027-8424
dc.identifier.issn
1091-6490
dc.identifier.other
10.1073/pnas.1920972117
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/407688
dc.identifier.doi
10.3929/ethz-b-000407688
dc.description.abstract
The Evening Complex (EC), composed of the DNA binding protein LUX ARRHYTHMO (LUX) and two additional proteins EARLY FLOWERING 3 (ELF3) and ELF4, is a transcriptional repressor complex and a core component of the plant circadian clock. In addition to maintaining oscillations in clock gene expression, the EC also participates in temperature and light entrainment, acting as an important environmental sensor and conveying this information to growth and developmental pathways. However, the molecular basis for EC DNA binding specificity and temperature-dependent activity were not known. Here, we solved the structure of the DNA binding domain of LUX in complex with DNA. Residues critical for high-affinity binding and direct base readout were determined and tested via site-directed mutagenesis in vitro and in vivo. Using extensive in vitro DNA binding assays of LUX alone and in complex with ELF3 and ELF4, we demonstrate that, while LUX alone binds DNA with high affinity, the LUX–ELF3 complex is a relatively poor binder of DNA. ELF4 restores binding to the complex. In vitro, the full EC is able to act as a direct thermosensor, with stronger DNA binding at 4 °C and weaker binding at 27 °C. In addition, an excess of ELF4 is able to restore EC binding even at 27 °C. Taken together, these data suggest that ELF4 is a key modulator of thermosensitive EC activity.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
National Academy of Sciences
en_US
dc.rights.uri
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject
circadian clock
en_US
dc.subject
gene regulation
en_US
dc.subject
Evening Complex
en_US
dc.subject
protein–DNA complex
en_US
dc.title
Molecular mechanisms of Evening Complex activity in Arabidopsis
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
dc.date.published
2020-03-12
ethz.journal.title
Proceedings of the National Academy of Sciences of the United States of America
ethz.journal.volume
117
en_US
ethz.journal.issue
12
en_US
ethz.journal.abbreviated
Proc Natl Acad Sci U S A
ethz.pages.start
6901
en_US
ethz.pages.end
6909
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Washington, DC
en_US
ethz.publication.status
published
en_US
ethz.date.deposited
2020-04-01T01:33:22Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2020-04-02T09:53:02Z
ethz.rosetta.lastUpdated
2022-03-29T01:43:37Z
ethz.rosetta.versionExported
true
ethz.COinS
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