Native mass spectrometry reveals the conformational diversity of the UVR8 photoreceptor
Open accessPublished version of a preprint
Abstract
Significance: The plant photoreceptor UVR8 absorbs UV-B light to regulate UV protection and photomorphogenic responses in plants. Here we show that UVR8 adopts multiple conformations to generate the signaling active state. The conformational diversity of UVR8 was revealed using a native mass spectrometry approach, where the photoreceptor was photoactivated in the ion source. Our analyses show that not only disordered but also ostensibly well-folded regions of UVR8 can adopt highly extended conformations that are likely to enhance interactions with partner proteins to facilitate signal propagation. The methodology employed could be used to investigate the structural dynamics of other proteins that are activated by light.
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The UVR8 photoreceptor in plants is crucial for generating photomorphogenic and protective responses to UV light.
“The UVR8 photoreceptor in plants is crucial for generating photomorphogenic and protective responses to UV light [162].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [162]
The UVR8 protein includes intrinsically disordered N- and C-terminal tails which regulate protein activity.
“The UVR8 protein includes intrinsically disordered N- and C-terminal tails which regulate protein activity [162].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [162]
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References 43 · Cited by 54
- Authors
- Camacho, I. S., Theisen, A., Johannissen, L. O., Díaz-Ramos, L. A., Christie, J. M., Jenkins, G. I., Bellina, B., Barran, P., & Jones, A. R.
- Affiliations
- National Physical Laboratory (GB)
- University of Manchester (GB)
- University of Glasgow (GB)
- Corresponding author
- Bellina, Bruno
- Barran, Perdita
- Jones, Alex R.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-01-04
- Volume
- 116
- Issue
- 4
- Pages
- 1116-1125
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6347689
- OpenAlex
- W2949236699
- Cited by
- 54
- References
- 43
- Citations by year
- 2026: 9 · 2025: 3 · 2024: 6 · 2023: 6 · 2022: 6 · 2021: 11 · 2020: 6 · 2019: 6 · 2018: 1
- FWCI
- 2.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion, cc-by)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion, cc-by-sa)
- Funders
- RCUK | Biotechnology and Biological Sciences Research Council (BB/L002655/1, BB/L016486/1)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Keywords
- UVR8, photoreceptor proteins, conformational heterogeneity, protein dimerization, photoactivation, C-terminal tail, intrinsically disordered regions, protein structural dynamics, Arabidopsis thaliana
- MeSH terms
- Chromosomal Proteins, Non-Histone, Light, Plant Proteins, Protein Conformation, Mass Spectrometry, Ultraviolet Rays, Catalytic Domain, Arabidopsis Proteins, Photoreceptors, Plant
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