ArticleACS synthetic biology2020
SPLIT: Stable Protein Coacervation Using a Light Induced Transition.
Article in ACS synthetic biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 58 citations in OpenAlex.
- Elucidating the Reciprocal Interplay between Supramolecular Polymer Cytoskeletons and Fuel-Dependent Synthetic Cells.Journal of the American Chemical Society · 2026Article
- Bottom-up Strategies for Generating Polymer Protocells That Mimic Cellular Communication.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Peptide Coacervates Can Protect Sequestered Oligonucleotides from Nucleases and Release Them for Transcription and Translation.Biomacromolecules · 2025Article
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- Article
- Rapid and reversible dissolution of biomolecular condensates using light-controlled recruitment of a solubility tag.Nature communications · 2024Article
- Rapid and reversible dissolution of biomolecular condensates using light-controlled recruitment of a solubility tag.bioRxiv : the preprint server for biology · 2024Article
- Emergent properties of melanin-inspired peptide/RNA condensates.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A Minispidroin Guides the Molecular Design for Cellular Condensation Mechanisms inACS synthetic biology · 2023Article
- Theoretical and Data-Driven Approaches for Biomolecular Condensates.Chemical reviews · 2023Review
- Biomolecular condensates formed by designer minimalistic peptides.Nature communications · 2023Article
- Protein Condensate Formation via Controlled Multimerization of Intrinsically Disordered Sequences.Biochemistry · 2022Article
- Modulating biomolecular condensates: a novel approach to drug discovery.Nature reviews. Drug discovery · 2022Review
- Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Incorporation and Assembly of a Light-Emitting Enzymatic Reaction into Model Protein Condensates.Biochemistry · 2021Article
- Designer membraneless organelles sequester native factors for control of cell behavior.Nature chemical biology · 2021Article
- Photocleavable proteins that undergo fast and efficient dissociation.Chemical science · 2021Article
- Signaling, Deconstructed: Using Optogenetics to Dissect and Direct Information Flow in Biological Systems.Annual review of biomedical engineering · 2021Review
- Designed and biologically active protein lattices.Nature communications · 2021Article
- Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Protein coacervates serve as hubs to concentrate and sequester proteins and nucleotides and thus function as membraneless organelles to manipulate cell physiology. We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light. Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light. We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain. Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions. An optimized version of this system displayed light-induced coacervation in
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Registered trials
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.