ArticleProceedings of the National Academy of Sciences of the United States of America2019
Native mass spectrometry reveals the conformational diversity of the UVR8 photoreceptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 52 citations in OpenAlex.
- Article
- Transcription factors interact with Arabidopsis UVR8 photoreceptor at distinct sites to COP1 and RUP proteins.The Plant journal : for cell and molecular biology · 2026Article
- Time-Resolved Native Mass Spectrometry Reveals Reversible Light-Driven Oligomerization of Arabidopsis Cryptochrome 1 and Its Antagonism by BIC1.Angewandte Chemie (International ed. in English) · 2026Article
- Characterization of Gas-Phase Native(-like) Proteins Using Structures for Lossless Ion Manipulations.Analytical chemistry · 2026Article
- Flavonoid pathway intermediates implicate UVR8 in functions beyond canonical UV-B signaling.Nature communications · 2025Article
- Conformational landscapes of rigid and flexible molecules explored with variable temperature ion mobility-mass spectrometry.Nature communications · 2025Article
- Recent advances in UV-B signalling: interaction of proteins with the UVR8 photoreceptor.Journal of experimental botany · 2025Review
- Genome-wide characterization of regulator of chromosome condensation 1 (RCC1) gene family in Artemisia annua L. revealed a conservation evolutionary pattern.BMC genomics · 2023Article
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- A seed-specific transcription factor, HSFA9, anticipates UV-B light responses by mimicking the activation of the UV-B receptor in tobacco.The Plant journal : for cell and molecular biology · 2022Article
- Cysteines have a role in conformation of the UVR8 photoreceptor.The Plant journal : for cell and molecular biology · 2022Article
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Biochemical characterization of the interaction between KRAS and Argonaute 2.Biochemistry and biophysics reports · 2022Article
- Intrinsically disordered proteins play diverse roles in cell signaling.Cell communication and signaling : CCS · 2022Review
- Dynamics and mechanism of dimer dissociation of photoreceptor UVR8.Nature communications · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- Article
- UV-B light and its application potential to reduce disease and pest incidence in crops.Horticulture research · 2021Review
- Tumor Susceptibility Gene 101 Regulates the Glucocorticoid Receptor through Disorder-Mediated Allostery.Biochemistry · 2021Article
- A "one pot" mass spectrometry technique for characterizing solution- and gas-phase photochemical reactions by electrospray mass spectrometry.RSC advances · 2021Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
UVR8 is a plant photoreceptor protein that regulates photomorphogenic and protective responses to UV light. The inactive, homodimeric state absorbs UV-B light, resulting in dissociation into monomers, which are considered to be the active state and comprise a β-propeller core domain and intrinsically disordered N- and C-terminal tails. The C terminus is required for functional binding to signaling partner COP1. To date, however, structural studies have only been conducted with the core domain where the terminal tails have been truncated. Here, we report structural investigations of full-length UVR8 using native ion mobility mass spectrometry adapted for photoactivation. We show that, while truncated UVR8 photoconverts from a single conformation of dimers to a single monomer conformation, the full-length protein exists in numerous conformational families. The full-length dimer adopts both a compact state and an extended state where the C terminus is primed for activation. In the monomer the extended C terminus destabilizes the core domain to produce highly extended yet stable conformations, which we propose are the fully active states that bind COP1. Our results reveal the conformational diversity of full-length UVR8. We also demonstrate the potential power of native mass spectrometry to probe functionally important structural dynamics of photoreceptor proteins throughout nature.
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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.