ArticleScience advances2023
Illuminating the inner workings of a natural protein switch: Blue-light sensing in LOV-activated diguanylate cyclases.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Extracellular Enzyme Activity and Growth of Chlorella sorokiniana in Response to COCurrent microbiology · 2026Article
- Integrating protein sequence design and evolutionary sequence conservation to uncover spectral tuning sites in red-light photoreceptors.Structure (London, England : 1993) · 2025Article
- Optogenetic enzymes: A deep dive into design and impact.Current opinion in structural biology · 2025Review
- Light-Driven Enzyme Catalysis: Ultrafast Mechanisms and Biochemical Implications.Biochemistry · 2025Review
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.The Journal of biological chemistry · 2025Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.bioRxiv : the preprint server for biology · 2025Article
- ESM-scan-A tool to guide amino acid substitutions.Protein science : a publication of the Protein Society · 2024Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Regulatory proteins play a crucial role in adaptation to environmental cues. Especially for lifestyle transitions, such as cell proliferation or apoptosis, switch-like characteristics are desirable. While nature frequently uses regulatory circuits to amplify or dampen signals, stand-alone protein switches are interesting for applications like biosensors, diagnostic tools, or optogenetics. However, such stand-alone systems frequently feature limited dynamic and operational ranges and suffer from slow response times. Here, we characterize a LOV-activated diguanylate cyclase (LadC) that offers precise temporal and spatial control of enzymatic activity with an exceptionally high dynamic range over four orders of magnitude. To establish this pronounced activation, the enzyme exhibits a two-stage activation process in which its activity is inhibited in the dark by caging its effector domains and stimulated upon illumination by the formation of an extended coiled-coil. These switch-like characteristics of the LadC system can be used to develop new optogenetic tools with tight regulation.
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Registered trials
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