Evidence map›Paper›PMID 32165537›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Molecular mechanisms of Evening Complex activity in

Catarina S Silva, Aditya Nayak, Xuelei Lai, Stephanie Hutin, Véronique Hugouvieux, Jae-Hoon Jung, Irene López-Vidriero, Jose M Franco-Zorrilla, Kishore C S Panigrahi, Max H Nanao and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
21.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

82 citing papers in PubMed, 161 citations in OpenAlex.

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22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 5 countries.

Catarina S SilvaLaboratoire de Physiologie Cellulaire and Végétale, Université Grenoble Alpes/Centre National de la Recherche Scientifique/Commissariat à l'Énergie Atomique et aux Énergies Alternatives/Institut National de la Recherche Agronomique/Interdisciplinary Research Institute of Grenoble, 38054 Grenoble, France; Csilva@embl.fr stephanie.hutin@univ-grenoble-alpes.fr Chloe.Zubieta@cea.fr.
Aditya NayakLaboratoire de Physiologie Cellulaire and Végétale, Université Grenoble Alpes/Centre National de la Recherche Scientifique/Commissariat à l'Énergie Atomique et aux Énergies Alternatives/Institut National de la Recherche Agronomique/Interdisciplinary Research Institute of Grenoble, 38054 Grenoble, France.
Xuelei LaiLaboratoire de Physiologie Cellulaire and Végétale, Université Grenoble Alpes/Centre National de la Recherche Scientifique/Commissariat à l'Énergie Atomique et aux Énergies Alternatives/Institut National de la Recherche Agronomique/Interdisciplinary Research Institute of Grenoble, 38054 Grenoble, France.
Stephanie HutinLaboratoire de Physiologie Cellulaire and Végétale, Université Grenoble Alpes/Centre National de la Recherche Scientifique/Commissariat à l'Énergie Atomique et aux Énergies Alternatives/Institut National de la Recherche Agronomique/Interdisciplinary Research Institute of Grenoble, 38054 Grenoble, France; Csilva@embl.fr stephanie.hutin@univ-grenoble-alpes.fr Chloe.Zubieta@cea.fr.
Véronique HugouvieuxLaboratoire de Physiologie Cellulaire and Végétale, Université Grenoble Alpes/Centre National de la Recherche Scientifique/Commissariat à l'Énergie Atomique et aux Énergies Alternatives/Institut National de la Recherche Agronomique/Interdisciplinary Research Institute of Grenoble, 38054 Grenoble, France.
Jae-Hoon JungDepartment of Biological Sciences, Sungkyunkwan University, 16419 Suwon, Korea.
Irene López-VidrieroGenomics Unit, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.
Jose M Franco-ZorrillaGenomics Unit, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.ORCID 0000-0001-6769-7349
Kishore C S PanigrahiPlant Biology Laboratory, School of Biological Sciences, National Institute of Science Education and Research, Bhubaneshwar, India 752050.
Max H NanaoStructural Biology Group, European Synchrotron Radiation Facility, 38043 Grenoble, France.
Philip A WiggeDepartment for Plant Adaptation, Leibniz-Institut für Gemüse- und Zierpflanzenbau, 14979 Grossbeeren, Germany.
Chloe ZubietaLaboratoire de Physiologie Cellulaire and Végétale, Université Grenoble Alpes/Centre National de la Recherche Scientifique/Commissariat à l'Énergie Atomique et aux Énergies Alternatives/Institut National de la Recherche Agronomique/Interdisciplinary Research Institute of Grenoble, 38054 Grenoble, France; Csilva@embl.fr stephanie.hutin@univ-grenoble-alpes.fr Chloe.Zubieta@cea.fr.ORCID 0000-0003-4558-9333
Centre National de la Recherche Scientifique · FRConsejo Superior de Investigaciones Científicas · ESEuropean Synchrotron Radiation Facility · FRLeibniz Institute of Vegetable and Ornamental Crops · DENational Institute of Science Education and Research · INSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Circadian RhythmGene Expression Regulation, PlantArabidopsisArabidopsis ProteinsDNA-Binding ProteinsDNA, PlantArabidopsis ProteinsDNA-Binding ProteinsDNA, Plantcircadian clockEvening Complexgene regulationprotein–DNA complex

Identifiers

PMID32165537
PMCPMC7104408
OpenAlexW3011295258

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.