Molecular dynamics simulations illuminate the role of sequence context in the ELF3-PrD-based temperature sensing mechanism in plants

Molecular dynamics simulations illuminate the role of sequence context in the ELF3-PrD-based temperature sensing mechanism in plants | bioRxiv Skip to main content Home About Submit ALERTS / RSS Search for this keyword Advanced Search New Results Molecular dynamics simulations illuminate the role of sequence context in the ELF3-PrD-based temperature sensing mechanism in plants Richard J. Lindsay , View ORCID Profile Abhilash Sahoo , Rafael Giordano Viegas , View ORCID Profile Vitor B. P. Leite , View ORCID Profile Philip A. Wigge , View ORCID Profile Sonya M. Hanson doi: https://doi.org/10.1101/2023.03.15.532793 Richard J. Lindsay 1 Center for Computational Biology, Flatiron Institute , New York, NY 10010, USA 2 Center for Computational Mathematics, Flatiron Institute , New York, NY 10010, USA Find this author on Google Scholar Find this author on PubMed Search for this author on this site Abhilash Sahoo 1 Center for Computational Biology, Flatiron Institute , New York, NY 10010, USA 2 Center for Computational Mathematics, Flatiron Institute , New York, NY 10010, USA Find this author on Google Scholar Find this author on PubMed Search for this author on this site ORCID record for Abhilash Sahoo Rafael Giordano Viegas 3 Department of Physics, São Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences , São José do Rio Preto, SP, 15054-000, Brazil 4 Federal Institute of Education, Science and Technology of São Paulo (IFSP) , Catanduva, São Paulo 15.808-305, Brazil Find this author on Google Scholar Find this author on PubMed Search for this author on this site Vitor B. P. Leite 3 Department of Physics, São Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences , São José do Rio Preto, SP, 15054-000, Brazil Find this author on Google Scholar Find this author on PubMed Search for this author on this site ORCID record for Vitor B. P. Leite Philip A. Wigge 5 Leibniz-Institut für Gemüse-und Zierpflanzenbau , Großbeeren, Germany 6 Institute of Biochemistry and Biology, University of Potsdam , Potsdam, Germany Find this author on Google Scholar Find this author on PubMed Search for this author on this site ORCID record for Philip A. Wigge Sonya M. Hanson 1 Center for Computational Biology, Flatiron Institute , New York, NY 10010, USA 2 Center for Computational Mathematics, Flatiron Institute , New York, NY 10010, USA Find this author on Google Scholar Find this author on PubMed Search for this author on this site ORCID record for Sonya M. Hanson For correspondence: shanson{at}flatironinstitute.org Abstract Full Text Info/History Metrics Supplementary material Data/Code Preview PDF Abstract The evening complex (EC) is a tripartite DNA repressor and a core component of the circadian clock that provides a mechanism for temperature-responsive growth and development of many plants. ELF3, a component of the EC, is a disordered scaffolding protein that blocks transcription of growth genes at low temperature. At increased temperature EC DNA binding is disrupted and ELF3 is sequestered in a reversible nuclear condensate, allowing transcription and growth to proceed. The condensation is driven by a low complexity prion-like domain (PrD), and the sensitivity of the temperature response is modulated by the length of a variable polyQ tract, with a longer polyQ tract corresponding to enhanced condensate formation and hypocotyl growth at increased temperature. Here, a series of computational studies provides evidence that polyQ tracts promote formation of temperature-sensitive helices in flanking residues with potential impacts for EC stability under increasing temperature. REST2 simulations uncover a heat-induced population of condensation-prone conformations that results from the exposure of ‘sticky’ aromatic residues by temperature-responsive breaking of long-range contacts. Coarse-grained Martini simulations reveal both polyQ tract length and sequence context modulate the temperature dependence of cluster formation. Understanding the molecular mechanism underlying the ELF3-PrD temperature response in plants has implications for technologies including modular temperature-response elements for heat-responsive protein design and agricultural advances to enable optimization of crop yields and allow plants to thrive in increasingly inhospitable environments. Competing Interest Statement The authors have declared no competing interest. Footnotes This version of the manuscript has been revised to update the analyses of the coarse-grained simulations. https://github.com/flatironinstitute/ELF3 https://users.flatironinstitute.org/~ccb/smbp/elf3_data/elf3prd_hcg.zip https://zenodo.org/doi/10.5281/zenodo.13226984 https://zenodo.org/doi/10.5281/zenodo.13285376 Funder Information Declared Simons Foundation, https://ror.org/01cmst727 , NA Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license . Back to top Previous Next Posted April 07, 2026. Download PDF Supplementary Material Data/Code Email Thank you for your interest in spreading the word about bioRxiv. NOTE: Your email address is requested solely to identify you as the sender of this article. Your Email * Your Name * Send To * Enter multiple addresses on separate lines or separate them with commas. You are going to email the following Molecular dynamics simulations illuminate the role of sequence context in the ELF3-PrD-based temperature sensing mechanism in plants Message Subject (Your Name) has forwarded a page to you from bioRxiv Message Body (Your Name) thought you would like to see this page from the bioRxiv website. Your Personal Message CAPTCHA This question is for testing whether or not you are a human visitor and to prevent automated spam submissions. Share Molecular dynamics simulations illuminate the role of sequence context in the ELF3-PrD-based temperature sensing mechanism in plants Richard J. Lindsay , Abhilash Sahoo , Rafael Giordano Viegas , Vitor B. P. Leite , Philip A. Wigge , Sonya M. Hanson bioRxiv 2023.03.15.532793; doi: https://doi.org/10.1101/2023.03.15.532793 Share This Article: Copy Citation Tools Molecular dynamics simulations illuminate the role of sequence context in the ELF3-PrD-based temperature sensing mechanism in plants Richard J. Lindsay , Abhilash Sahoo , Rafael Giordano Viegas , Vitor B. P. Leite , Philip A. Wigge , Sonya M. Hanson bioRxiv 2023.03.15.532793; doi: https://doi.org/10.1101/2023.03.15.532793 Citation Manager Formats BibTeX Bookends EasyBib EndNote (tagged) EndNote 8 (xml) Medlars Mendeley Papers RefWorks Tagged Ref Manager RIS Zotero Tweet Widget Facebook Like Google Plus One Subject Area Biophysics Subject Areas All Articles Animal Behavior and Cognition (8003) Biochemistry (18709) Bioengineering (14841) Bioinformatics (44360) Biophysics (22560) Cancer Biology (19680) Cell Biology (26844) Clinical Trials (138) Developmental Biology (13942) Ecology (20969) Epidemiology (2067) Evolutionary Biology (25412) Genetics (16151) Genomics (23477) Immunology (18678) Microbiology (42413) Molecular Biology (18021) Neuroscience (93343) Paleontology (699) Pathology (2977) Pharmacology and Toxicology (5086) Physiology (8105) Plant Biology (15969) Scientific Communication and Education (2094) Synthetic Biology (4549) Systems Biology (10219) Zoology (2384)

Related documents

• Adaptive response to long-term high temperatures during the reproductive development in Arabidopsis thaliana.#425134
• Diel rewiring and positive selection of ancient plant proteins enabled evolution of CAM photosynthesis in Agave#492016
• From greenhouse climate to individual leaves: an organ-resolved model of lettuce growth#1063329
• Phytohormone-Mediated Regulation of Plant Cold Stress Tolerance: Signaling, Hormonal Crosstalk, and Translational Perspectives#253701
• Integrating multi-omics approaches to shape legume root system architecture under drought stress: a comprehensive review.#247748